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Arthropod defensins illuminate the divergence of scorpion neurotoxins
Author(s) -
Froy Oren,
Gurevitz Michael
Publication year - 2004
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.578
Subject(s) - scorpion , biology , venom , scorpion venoms , arthropod , intron , gene , phylogenetic tree , genetics , defensin , insect , phylogenetics , exon , evolutionary biology , botany , biochemistry , paleontology
Defensins are phylogenetically ancient antibacterial polypeptides found in plants and animals. Isolation of the cDNA and genomic sequences encoding the scorpion ( Leiurus quinquestriatus hebraeus ) defensin revealed similarity to scorpion neurotoxins in gene organization (two exons and a phase I intron) and intron characteristics (conserved acceptor, donor and putative branch sites). This commonality, alongside a similar core structure, protein sequence and bioactivity suggest that arthropod defensins and scorpion neurotoxins share a common ancestor. Interestingly, phylogenetic analysis of defensins and scorpion neurotoxins illuminates for the first time a putative evolutionary trajectory for scorpion sodium and potassium channel neurotoxins. Copyright © 2004 European Peptide Society and John Wiley & Sons, Ltd.