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Structures of genes for two cathelin‐associated antimicrobial peptides: prophenin‐2 and PR‐39
Author(s) -
Zhao Chengquan,
Ganz Tomas,
Lehrer Robert I.
Publication year - 1995
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(95)01237-3
Subject(s) - exon , intron , gene , biology , genetics , antimicrobial peptides , microbiology and biotechnology , peptide , gene family , exon shuffling , valine , peptide sequence , antimicrobial , tandem exon duplication , amino acid , biochemistry , gene expression
We characterized genes for prophenin (PF)‐2 and PR‐39, two cathelin‐associated antimicrobial peptides found in porcine leukocytes. Both contained 4 exons and 3 introns and were compact, contiguous and highly homologous. Exons I–III encoded most of their cathelin domains. Exon IV specified the final few cathelin residues, including its conserved C‐terminal valine, followed by the mature PR‐39 peptide or a PF‐2 precursor. The highly conserved 5′ flanking sequences of this gene family contained NF‐κB, IL‐6, GM‐CSF and NF‐1 binding motifs and the introns were unusually conserved. These data suggest that the panoply of porcine cathelin‐associated antimicrobial peptides arose relatively recently via gene reduplications and exon shuffling, and that in vivo expression of cathelin‐associated antimicrobial peptides may respond to mediators generated early during infection.