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Sequence and evolution of a hexamerin from the ant Camponotus festinatus
Author(s) -
Martínez T.,
Burmester T.,
Veenstra J. A.,
Wheeler Diana
Publication year - 2000
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 - 10.1046/j.1365-2583.2000.00204.x
Subject(s) - biology , braconidae , phylogenetic tree , phylogenetics , ant , brood , asparagine , amino acid , zoology , storage protein , hymenoptera , evolutionary biology , ecology , gene , biochemistry , parasitoid
In the ant Camponotus festinatus, two different hexamerins accumulate stage‐specifically during the late larval period and at various times in adults. These hexamerins serve as storage proteins and play important roles in brood nourishment and colony founding. We report an analysis of the cDNA sequence of C. festinatus hexamerin 2 (CfeHex2). The native protein contains 732 amino acids, which are moderately enriched in aromatic amino acids, aspartate and asparagine. Phylogenetic analyses show a close relationship of CfeHex2 to a putative toxin of the braconid wasp, Bracon hebetor. The divergence of Formicidae and Braconidae hexamerins was calculated to have begun 187 MYA, an estimate consistent with currently accepted phylogeny of insect orders.