Evidence for recurrent paralogous gene conversion and exceptional allelic divergence in the Attacin genes of Drosophila melanogaster.
Insects produce a limited variety of antibacterial peptides to combat a wide diversity of pathogens. These peptides are often conserved across evolutionarily distant taxa, but little is known about the level and structure of polymorphism within species. We have surveyed naturally occurring genetic variation in the promoter and coding regions of three Attacin antibacterial peptide genes from 12 lines of Drosophila melanogaster. These genes exhibit high levels of silent nucleotide variations (1-3% per nucleotide heterozygosity), but are not excessively polymorphic at the amino acid level. There is extensive variation in the Attacin promoters, some of which may affect transcriptional efficiency, and one line carries a deletion in the Attacin A coding region that renders this gene nonfunctional. Two of the genes, Attacins A and B, are arranged in tandem and show evidence of repeated interlocus gene conversion. Attacin C, more divergent and located 1.3 Mbp upstream of Attacins A and B, does not appear to have been involved in such exchanges. All three genes are characterized by divergent haplotypes, and one Attacin AB allele appears to have recently increased rapidly in frequency in the population.
Lazzaro
B P
BP
Institute of Molecular Evolutionary Genetics, Department of Biology, Penn State University, University Park, Pennsylvania 16802, USA. bplazzaro@psu.edu
Clark
A G
AG
D000483:Alleles; D000595:Amino Acid Sequence; D000818:Animals; D029721:Drosophila Proteins; D004331:Drosophila melanogaster / Q000235:genetics*; D005785:Gene Conversion; D005786:Gene Expression Regulation; D019476:Insect Proteins / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
C488990:AttA protein, Drosophila; C488991:AttB protein, Drosophila; C488989:AttC protein, Drosophila; D029721:Drosophila Proteins; D019476:Insect Proteins; C039711:attacin antibacterial protein, insect