Comparison of fibroin cDNAs from webspinning insects: insight into silk formation and function

Zoology (Jena). 2011 Sep;114(4):239-46. doi: 10.1016/j.zool.2011.01.004. Epub 2011 Jul 8.

Abstract

Embiopterans (webspinning insects) are renowned for their prolific use of silk. These organisms spin silk to construct elaborate networks of tubes in which they live, forage, and reproduce. The silken galleries are essential for protecting these soft-bodied insects from predators and other environmental hazards. Despite the ecological importance of embiopteran silk, very little is known about its constituent proteins. Here, we characterize the silk protein cDNAs from four embiopteran species to better understand the function and evolution of these adaptive molecules. We show that webspinner fibroins (silk proteins) are highly repetitive in sequence and possess several conserved characteristics, despite differences in habitat preferences across species. The most striking similarities are in the codon usage biases of the fibroin genes, particularly in the repetitive regions, as well as sequence conservation of the carboxyl-terminal regions of the fibroins. Based on analyses of the silk genes, we propose hypotheses regarding codon bias and its effect on the translation and replication of these unusual genes. Furthermore, we discuss the significance of specific fibroin motifs to the mechanical and structural characteristics of silk fibers. Lastly, we report that the conservation of webspinner fibroin carboxyl-terminal regions suggests that fiber formation may occur through a mechanism analogous to that found in Lepidoptera. From these results, insight is gained into the tempo and mode of evolution that has shaped embiopteran fibroins.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Codon
  • Conserved Sequence
  • DNA, Complementary / chemistry
  • Evolution, Molecular
  • Female
  • Fibroins / genetics*
  • Insecta / genetics*
  • Molecular Sequence Data
  • Protein Structure, Secondary
  • Silk / chemistry
  • Silk / genetics*

Substances

  • Codon
  • DNA, Complementary
  • Silk
  • Fibroins