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Organization, evolution and transcriptional profile of hexamerin genes of the parasitic wasp Nasonia vitripennis (Hymenoptera: Pteromalidae)
Author(s) -
Cristino A. S.,
Nunes F. M. F.,
Barchuk A. R.,
AguiarCoelho V. M.,
Simões Z. L. P.,
Bitondi M. M. G.
Publication year - 2010
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/j.1365-2583.2009.00970.x
Subject(s) - nasonia vitripennis , pteromalidae , biology , hymenoptera , parasitoid wasp , gene , insect , evolutionary biology , botany , genetics , parasitoid
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.