6533b830fe1ef96bd1296780

RESEARCH PRODUCT

Sequence and evolution of a hexamerin from the ant Camponotus festinatus.

Jan A. VeenstraJan A. VeenstraThorsten BurmesterDiana E. WheelerTeresa Martinez

subject

Camponotus festinatusDNA ComplementarySequence analysisBracon hebetormedia_common.quotation_subjectMolecular Sequence DataZoologyInsectEvolution MolecularPhylogeneticsGeneticsAnimalsAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenymedia_commonbiologyBase SequenceSequence Homology Amino AcidEcologyAntsfungibiology.organism_classificationBroodInsect ScienceInsect ProteinsBraconidaeSequence Analysis

description

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.

yearjournalcountryeditionlanguage
2000-09-06Insect molecular biology
10.1046/j.1365-2583.2000.00204.xhttps://pubmed.ncbi.nlm.nih.gov/10971720