Organization, evolution and transcriptional profile of hexamerin genes of the parasitic wasp Nasonia vitripennis (Hymenoptera: Pteromalidae)

Insect Mol Biol. 2010 Feb:19 Suppl 1:137-46. doi: 10.1111/j.1365-2583.2009.00970.x.

Abstract

Hexamerins and prophenoloxidases (PPOs) proteins are members of the arthropod-haemocyanin superfamily. In contrast to haemocyanin and PPO, hexamerins do not bind oxygen, but mainly play a role as storage proteins that supply amino acids for insect metamorphosis. We identified seven genes encoding hexamerins, three encoding PPOs, and one hexamerin pseudogene in the genome of the parasitoid wasp Nasonia vitripennis. A phylogenetic analysis of hexamerins and PPOs from this wasp and related proteins from other insect orders suggests an essentially order-specific radiation of hexamerins. Temporal and spatial transcriptional profiles of N. vitripennis hexamerins suggest that they have physiological functions other than metamorphosis, which are arguably coupled with its lifestyle.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bayes Theorem
  • Catechol Oxidase / genetics*
  • Computational Biology
  • DNA Primers / genetics
  • Enzyme Precursors / genetics*
  • Evolution, Molecular*
  • Gene Components
  • Gene Expression Profiling
  • Insect Proteins / genetics*
  • Insect Proteins / metabolism*
  • Models, Genetic
  • Phylogeny*
  • Reverse Transcriptase Polymerase Chain Reaction
  • Species Specificity
  • Wasps / genetics*

Substances

  • DNA Primers
  • Enzyme Precursors
  • Insect Proteins
  • storage proteins, Insecta
  • pro-phenoloxidase
  • Catechol Oxidase