Toxins 2017, 9(1), 10; https://doi.org/10.3390/toxins9010010
Exon Shuffling and Origin of Scorpion Venom Biodiversity
Group of Peptide Biology and Evolution, State Key Laboratory of Integrated Management of Pest Insects & Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, Beijing 100101, China
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Academic Editor: Bryan Grieg Fry
Received: 26 July 2016 / Revised: 13 December 2016 / Accepted: 21 December 2016 / Published: 26 December 2016
(This article belongs to the Collection Evolution of Venom Systems)
Abstract
Scorpion venom is a complex combinatorial library of peptides and proteins with multiple biological functions. A combination of transcriptomic and proteomic techniques has revealed its enormous molecular diversity, as identified by the presence of a large number of ion channel-targeted neurotoxins with different folds, membrane-active antimicrobial peptides, proteases, and protease inhibitors. Although the biodiversity of scorpion venom has long been known, how it arises remains unsolved. In this work, we analyzed the exon-intron structures of an array of scorpion venom protein-encoding genes and unexpectedly found that nearly all of these genes possess a phase-1 intron (one intron located between the first and second nucleotides of a codon) near the cleavage site of a signal sequence despite their mature peptides remarkably differ. This observation matches a theory of exon shuffling in the origin of new genes and suggests that recruitment of different folds into scorpion venom might be achieved via shuffling between body protein-coding genes and ancestral venom gland-specific genes that presumably contributed tissue-specific regulatory elements and secretory signal sequences. View Full-Text
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Wang, X.; Gao, B.; Zhu, S. Exon Shuffling and Origin of Scorpion Venom Biodiversity. Toxins 2017, 9, 10.
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