title: Relationship of promagainin to three other prohormones from the skin of Xenopus laevis: a different perspective.
abstract: We observed a striking sequence similarity between precursors for promagainin and procaerulein type I (excluding the caerulein peptide region). Additional comparisons of the promagainin precursor with those of other procaeruleins, proxenopsin, and peptide-Gly-Leu-amide revealed that all possess one or more copies of a structurally similar spacer module, from which an amphiphilic spacer peptide is cleaved. Promagainin yields the magainins, spacer peptides with antimicrobial activity; we suggest other spacer peptides may have similar activity. We propose that the genes for the four kinds of hormones were derived from a common ancestral gene through gene and exon duplications and that the procaerulein and proxenopsin genes are mosaic genes in which the original 3'-ends were replaced by exon shuffling.
authors: National Biomedical Research Foundation, Georgetown University Medical Center, Washington, DC 20007.
authors: L T
authors: LT
authors: Hunt
authors: W C
authors: WC
authors: Barker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D002108:Ceruletide / Q000235:genetics; D006728:Hormones / Q000235:genetics* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000235:genetics; D010455:Peptides / Q000235:genetics / Q000302:isolation & purification; D011498:Protein Precursors / Q000235:genetics* / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D012867:Skin / Q000378:metabolism*; D012984:Software; D029867:Xenopus Proteins; D014982:Xenopus laevis / Q000502:physiology*
chemical_list: D023181:Antimicrobial Cationic Peptides; D006728:Hormones; D009842:Oligopeptides; D010455:Peptides; D011498:Protein Precursors; D029867:Xenopus Proteins; C118273:procaerulein; C045866:peptide-Gly-Leu-amide; C056453:promagainin protein, Xenopus; C016832:xenopsin; D002108:Ceruletide