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Structural changes under low evolutionary constraint may decrease the affinity of dibenzoylhydrazine insecticides for the ecdysone receptor in non-lepidopteran insects

Moises João Zotti UGent, Olivier Christiaens UGent, Pierre Rougé, Anderson Grutzmacher, Paulo Zimmer and Guy Smagghe UGent (2012) INSECT MOLECULAR BIOLOGY. 21(5). p.488-501
abstract
Understanding how variations in genetic sequences are conveyed into structural and biochemical properties is of increasing interest in the field of molecular evolution. In order to gain insight into this process, we studied the ecdysone receptor (EcR), a transcription factor that controls moulting and metamorphosis in arthropods. Using an in silico homology model, we identified a region in the lepidopteran EcR that has no direct interaction with the natural hormone but is under strong evolutionary constraint. This region causes a small indentation in the three-dimensional structure of the protein which facilitates the binding of tebufenozide. Non-Mecopterida are considered much older, evolutionarily, than Lepidoptera and they do not have this extended cavity. This location shows differences in evolutionary constraint between Lepidoptera and other insects, where a much lower constraint is observed compared with the Lepidoptera. It is possible that the higher flexibility seen in the EcR of Lepidoptera is an entirely new trait and the higher constraint could then be an indication that this region does have another important function. Finally, we suggest that Try123, which is evolutionarily constrained and is up to now exclusively present in Lepidoptera EcRs, could play a critical role in discriminating between steroidal and non-steroidal ligands.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ECR REPORTER ASSAYS, DROSOPHILA CELL-LINE, NUCLEAR RECEPTORS, PROTEIN SEQUENCES, RAPID DIVERGENCE, RESIDUES, USP, SUBSTITUTIONS, CONSERVATION, evolutionary constraint, differential binding, LIGAND-BINDING DOMAIN, dibenzoylhydrazine, molecular evolution, ecdysone receptor
journal title
INSECT MOLECULAR BIOLOGY
Insect Mol. Biol.
volume
21
issue
5
pages
488 - 501
Web of Science type
Article
Web of Science id
000308582100002
JCR category
ENTOMOLOGY
JCR impact factor
3.044 (2012)
JCR rank
3/87 (2012)
JCR quartile
1 (2012)
ISSN
0962-1075
DOI
10.1111/j.1365-2583.2012.01154.x
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
2106346
handle
http://hdl.handle.net/1854/LU-2106346
date created
2012-05-14 17:55:26
date last changed
2013-07-12 12:03:51
@article{2106346,
  abstract     = {Understanding how variations in genetic sequences are conveyed into structural and biochemical properties is of increasing interest in the field of molecular evolution. In order to gain insight into this process, we studied the ecdysone receptor (EcR), a transcription factor that controls moulting and metamorphosis in arthropods. Using an in silico homology model, we identified a region in the lepidopteran EcR that has no direct interaction with the natural hormone but is under strong evolutionary constraint. This region causes a small indentation in the three-dimensional structure of the protein which facilitates the binding of tebufenozide. Non-Mecopterida are considered much older, evolutionarily, than Lepidoptera and they do not have this extended cavity. This location shows differences in evolutionary constraint between Lepidoptera and other insects, where a much lower constraint is observed compared with the Lepidoptera. It is possible that the higher flexibility seen in the EcR of Lepidoptera is an entirely new trait and the higher constraint could then be an indication that this region does have another important function. Finally, we suggest that Try123, which is evolutionarily constrained and is up to now exclusively present in Lepidoptera EcRs, could play a critical role in discriminating between steroidal and non-steroidal ligands.},
  author       = {Zotti, Moises Jo{\~a}o and Christiaens, Olivier and Roug{\'e}, Pierre and Grutzmacher, Anderson and Zimmer, Paulo and Smagghe, Guy},
  issn         = {0962-1075},
  journal      = {INSECT MOLECULAR BIOLOGY},
  keyword      = {ECR REPORTER ASSAYS,DROSOPHILA CELL-LINE,NUCLEAR RECEPTORS,PROTEIN SEQUENCES,RAPID DIVERGENCE,RESIDUES,USP,SUBSTITUTIONS,CONSERVATION,evolutionary constraint,differential binding,LIGAND-BINDING DOMAIN,dibenzoylhydrazine,molecular evolution,ecdysone receptor},
  language     = {eng},
  number       = {5},
  pages        = {488--501},
  title        = {Structural changes under low evolutionary constraint may decrease the affinity of dibenzoylhydrazine insecticides for the ecdysone receptor in non-lepidopteran insects},
  url          = {http://dx.doi.org/10.1111/j.1365-2583.2012.01154.x},
  volume       = {21},
  year         = {2012},
}

Chicago
Zotti, Moises João, Olivier Christiaens, Pierre Rougé, Anderson Grutzmacher, Paulo Zimmer, and Guy Smagghe. 2012. “Structural Changes Under Low Evolutionary Constraint May Decrease the Affinity of Dibenzoylhydrazine Insecticides for the Ecdysone Receptor in Non-lepidopteran Insects.” Insect Molecular Biology 21 (5): 488–501.
APA
Zotti, M. J., Christiaens, O., Rougé, P., Grutzmacher, A., Zimmer, P., & Smagghe, G. (2012). Structural changes under low evolutionary constraint may decrease the affinity of dibenzoylhydrazine insecticides for the ecdysone receptor in non-lepidopteran insects. INSECT MOLECULAR BIOLOGY, 21(5), 488–501.
Vancouver
1.
Zotti MJ, Christiaens O, Rougé P, Grutzmacher A, Zimmer P, Smagghe G. Structural changes under low evolutionary constraint may decrease the affinity of dibenzoylhydrazine insecticides for the ecdysone receptor in non-lepidopteran insects. INSECT MOLECULAR BIOLOGY. 2012;21(5):488–501.
MLA
Zotti, Moises João, Olivier Christiaens, Pierre Rougé, et al. “Structural Changes Under Low Evolutionary Constraint May Decrease the Affinity of Dibenzoylhydrazine Insecticides for the Ecdysone Receptor in Non-lepidopteran Insects.” INSECT MOLECULAR BIOLOGY 21.5 (2012): 488–501. Print.