Title: | Molecular diversity of PBAN family peptides from fire ants |
Author(s): | Choi MY; Vander Meer RK; Valles SM; |
Address: | "United States Department of Agriculture-Agricultural Research Service, Center of Medical, Agricultural and Veterinary Entomology (CMAVE), Gainesville, Florida 32608, USA. mychoi@ars.usda.gov" |
Journal Title: | Arch Insect Biochem Physiol |
ISSN/ISBN: | 1520-6327 (Electronic) 0739-4462 (Linking) |
Abstract: | "The PBAN/Pyrokinin peptide family is a major neuropeptide family characterized with a common FXPRLamide in the C-termini. These peptides are ubiquitously distributed in the Insecta and are involved in many essential endocrinal functions, e.g., pheromone production. Previous work demonstrated the localization of PBAN in the fire ant central nervous system, and identified a new family of PBAN from the red imported fire ant, Solenopsis invicta. In this study, we identified five more PBAN/Pyrokinin genes from S. geminata, S. richteri, S. pergandii, S. carolinensis, and a hybrid of S. invicta and S. richteri. The gene sequences were used to determine the phylogenetic relationships of these species and hybrid, which compared well to the morphologically defined fire ant subgroup complexes. The putative PBAN and other peptides were determined from the amino acid sequences of the PBAN/pyrokinin genes. We summarized all known insect PBAN family neuropeptides, and for the first time constructed a phylogenetic tree based on the full amino acid sequences translated from representative PBAN cDNAs. The PBAN/pyrokinin gene is well conserved in Insecta and probably extends into the Arthropod phylum; however, translated pre-propeptides may vary and functional diversity may be retained, lost, or modified during the evolutionary process" |
Keywords: | "Amino Acid Sequence Animals Ants/*genetics/*physiology Base Sequence DNA, Complementary/genetics Molecular Sequence Data Neuropeptides/*genetics/*metabolism;" |
Notes: | "MedlineChoi, Man-Yeon Vander Meer, Robert K Valles, Steven M eng 2010/06/01 Arch Insect Biochem Physiol. 2010 Jun; 74(2):67-80. doi: 10.1002/arch.20356" |