Resilin, the gene for the molecular spring: its roles in the flight and jumpingof Drosophila

Abstract

Resilin is a member of the chitin-binding protein family that was originally found as a major component of an elastic matrix present in insects. The knockdown of the gene for this protein in Drosophila melanogaster causes the characteristic downturned wing posture, and the knockdown flies cannot move their wings. The jump distance of the knockdown flies is around 50% shorter than that of the controls. Null mutant flies show the same phenotypes, which can be rescued by introducing a 4.7 kb genomic fragment harboring the whole coding region of Resilin. In vitro experiments have shown that the elasticity of the matrix made of Resilin is due to the dityrosine-mediated polymerization of Resilin molecules. Dual oxidase (Duox) is the most likely candidate for the in vivo polymerization of Resilin molecules. Duox knockdown induces phenotypes similar to those observed in wing posture and jump performance of the Resilin knockdown and knockout flies, which can be rescued by the overexpression of Duox gene from a beetle. These findings suggest that Duox is an essential factor for the proper function of Resilin as the major component of the resilin matrix.