Abstract
We report that the drosulfakinin 0 (DSK 0; NQKTMSFNH2) structure and genomic organization are conserved. The DSK 0 C-terminus, SFNH2, is widely distributed in the animal kingdom suggesting it defines a novel peptide family. We also report the first description of DSK 0 activity. DSK 0, I (DSK I, FDDYGHMRFNH2), and II (DSK II, GGDDQFDDYGHMRFNH2) are encoded in sulfakinin (Dsk). Drosophila erecta, Drosophila sechellia, Drosophila simulans, and Drosophila yakuba shared 62.5-87.5% identity to Drosophila melanogaster DSK 0; Drosophila pseudoobscura shared 37.5% identity; numerous amino acids were one nucleotide different from a corresponding residue in D. melanogaster. DSK I and II were identical among the drosopholids. DSK 0 proteolytic processing sites were RR except D. yakuba contained KR and D. pseudoobscura contained HR, one nucleotide different from RR. DSK I and II processing sites were identical among the drosopholids. We established DSK 0 decreased adult (EC50=237nM and R(2)=0.941), but not larval gut contractions. DSK 0 exists in the central nervous system including the subesophageal ganglion and an abdominal ganglion. Peptide and genomic conservation, activity, and spatial and temporal distribution support the conclusion that DSK 0 plays diverse biological roles in drosopholids including regulating gut muscle contraction.
