Premium
Structure of the yellow sac spider C heiracanthium punctorium genes provides clues to evolution of insecticidal two‐domain knottin toxins
Author(s) -
Sachkova M. Y.,
Slavokhotova A. A.,
Grishin E. V.,
Vassilevski A. A.
Publication year - 2014
Publication title -
insect molecular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.955
H-Index - 93
eISSN - 1365-2583
pISSN - 0962-1075
DOI - 10.1111/imb.12097
Subject(s) - biology , gene , genetics , negative selection , exon shuffling , protein domain , exon , intron , computational biology , evolutionary biology , genome , alternative splicing
Abstract Yellow sac spiders ( C heiracanthium punctorium , family M iturgidae) are unique in terms of venom composition, because, as we show here, two‐domain toxins have replaced the usual one‐domain peptides as the major constituents. We report the structure of the two‐domain Che . punctorium toxins ( CpTx ), along with the corresponding cDNA and genomic DNA sequences. At least three groups of insecticidal CpTx were identified, each consisting of several members. Unlike many cone snail and snake toxins, accelerated evolution is not typical of cptx genes, which instead appear to be under the pressure of purifying selection. Both CpTx modules present the inhibitor cystine knot ( ICK ), or knottin signature; however, the sequence similarity between the domains is low. Conversely, notable similarity was found between separate domains of CpTx and one‐domain toxins from spiders of the L ycosidae family. The observed chimerism is a landmark of exon shuffling events, but in contrast to many families of multidomain protein genes no introns were found in the cptx genes. Considering the possible scenarios, we suggest that an early transcription‐mediated fusion event between two related one‐domain toxin genes led to the emergence of a primordial cptx ‐like sequence. We conclude that evolution of toxin variability in spiders appears to be quite different from other venomous animals.