Isolation and characterization of a Drosophila neuropeptide gene.
We have purified a 9 amino acid amidated neuropeptide, DPKQDFMRFamide, from whole adult D. melanogaster. This peptide exhibits sequence homology to the molluscan bioactive tetrapeptide FMRFamide and is a novel member of the FMRFamide peptide family. The gene encoding DPKQDFMRFamide has been cloned and characterized. It is present in a single copy per haploid genome, is expressed as a unique 1.7 kb mRNA species, and cytologically maps to 46C on the right arm of chromosome 2. Characterization of a cDNA clone indicates that the precursor protein is 347 amino acids in length and contains 5 copies of DPKQDFMRFamide, as well as 10 additional amidated peptides exhibiting varying degrees of structural relatedness. The Drosophila DPKQDFMRFamide gene and the Aplysia FMRFamide gene are ancestrally related; however, peptides display a higher degree of homology within a species than between species, suggesting intragenic concerted evolution of these neuropeptides.
Nambu
J R
JR
Department of Biological Sciences, Stanford University, California 94305.
Murphy-Erdosh
C
C
Andrews
P C
PC
Feistner
G J
GJ
Scheller
R H
RH
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D004330:Drosophila / Q000235:genetics*; D019835:FMRFamide; D005796:Genes; D008969:Molecular Sequence Data; D009479:Neuropeptides / Q000235:genetics*
D009479:Neuropeptides; D019835:FMRFamide