Meeting Abstract

P2.31  Thursday, Jan. 5  Variation In Projectin Isoforms and Flight Performance In Drosophila melanogaster. CORDER, Katelynn M*; AYME-SOUTHGATE, Agnes J; College of Charleston, Charleston

Insect flight muscles are extraordinary in their diversity at the anatomical, physiological and molecular levels. The myofibrillar structure provides the muscle with its contractile properties and contributes to muscle stiffness. Insect sarcomeres contain short, relatively inextensible filaments linking the Z-band to the myosin contractile filaments, which are known as C-filaments and contain two extremely large proteins, projectin and kettin/Sls. The molecular characterization of projectin in basal and derived insects reveals a highly conserved modular organization, including immunoglobulin and fibronectin domains together with a unique PEVK region. The PEVK domain is extensively alternatively spliced, giving rise to isoforms with PEVK regions ranging from 100 to 600 amino acids in D. melanogaster. The unusual amino acid composition of the PEVK segment, as well as its variable length may contribute to its proposed role as the elastic segment in the projecin protein. We investigated the possible correlation between the relative abundance of different projectin PEVK isoforms and parameters that are known to affect the fly’s flight property. We will present data to determine the presence and ratio of different projectin PEVK isoforms under different conditions such as age, sex, and flight impairment by mutations or manipulations.