Molecular Analysis of the Muscle Protein Projectin in Lepidoptera
Author(s) -
Agnes Ayme-Southgate,
Lynda Turner,
Richard Southgate
Publication year - 2013
Publication title -
journal of insect science
Language(s) - English
Resource type - Journals
ISSN - 1536-2442
DOI - 10.1673/031.013.8801
Subject(s) - lepidoptera genitalia , biology , danaus , sphingidae , manduca sexta , bombycidae , manduca , titin , nymphalidae , saturniidae , monarch butterfly , insect , evolutionary biology , bombyx mori , zoology , botany , sarcomere , genetics , microbiology and biotechnology , gene , myocyte
Striated muscles of both vertebrates and insects contain a third filament composed of the giant proteins, namely kettin and projectin (insects) and titin (vertebrates). All three proteins have been shown to contain several domains implicated in conferring elasticity, in particular a PEVK segment. In this study, the characterization of the projectin protein in the silkmoth, Bombyx mori L. (Lepidoptera: Bombycidae), and the monarch butterfly, Danaus plexippus L. (Lepidoptera: Nymphalidae), as well as a partial characterization in the Carolina sphinx, Manduca sexta L. (Lepidoptera: Sphingidae), are presented. This study showed that, similar to other insects, projectin's overall modular organization was conserved, but in contrast, the PEVK region had a highly divergent sequence. The analysis of alternative splicing in the PEVK region revealed a small number of possible isoforms and the lack of a flight-muscle specific variant, both characteristics being in sharp contrast with findings from other insects. The possible correlation with difference in flight muscle stiffness and physiology between Lepidoptera and other insect orders is discussed.
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