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Relationship of promagainin to three other prohormones from the skin of Xenopus laevis : A different perspective
Author(s) -
Hunt Lois T.,
Barker Wia C.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80443-5
Subject(s) - xenopus , perspective (graphical) , neuroscience , biology , computer science , biochemistry , artificial intelligence , gene
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.