Journal
FEBS LETTERS
Volume 588, Issue 5, Pages 740-745Publisher
WILEY
DOI: 10.1016/j.febslet.2014.01.018
Keywords
Molecular evolution; Spider venom gland; Inhibitor cystine knot (ICK); cDNA library; Toxin gene
Funding
- Russian Foundation for Basic Research [11-04-00706, 12-0433151]
- Program of Molecular and Cell Biology of the Russian Academy of Sciences
- Ministry of Education and Science of the Russian Federation [8794]
- Russian Federation
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Spiderines are comparatively long polypeptide toxins (similar to 110 residues) from lynx spiders (genus Oxyopes). They are built of an N-terminal linear cationic domain (similar to 40 residues) and a C-terminal knottin domain (similar to 60 residues). The linear domain empowers spiderines with strong cytolytic activity. In the present work we report 16 novel spiderine sequences from Oxyopes takobius and Oxyopes lineatus classified into two subfamilies. Strikingly, negative selection acts on both linear and knottin domains. Genes encoding Oxyopes two-domain toxins were sequenced and found to be intronless. We further discuss a possible scenario of lynx spider modular toxin evolution. (c) 2014 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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