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

Autor: Cristino AS; The Queensland Brain Institute, The University of Queensland, Brisbane, Queensland, Australia. a.cristino@uq.edu.au, Nunes FM, Barchuk AR, Aguiar-Coelho VM, Simões ZL, Bitondi MM
Jazyk: angličtina
Zdroj: Insect molecular biology [Insect Mol Biol] 2010 Feb; Vol. 19 Suppl 1, pp. 137-46.
DOI: 10.1111/j.1365-2583.2009.00970.x
Abstrakt: 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.
Databáze: MEDLINE