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Published on: August 23, 2018
Adaptive evolution of cry genes in Bacillus thuringiensis: implications for their specificity determination
Jin-Yu Wu1, Fang-Qing Zhao, Jie Bai
1Institute of Biomedical Informatics, Wenzhou Medical College, Wenzhou 325000, China.
Genomics, Proteomics & Bioinformatics
|September 26, 2007
Summary
Bacillus thuringiensis Cry proteins evolve adaptively, with 24 key residues in Domains II and III driving insect specificity. This evolution likely results from an "arms race" with targeted insects, leading to functional divergence.
Area of Science:
- * Molecular biology and evolutionary genetics.
- * Biochemistry and entomology.
Background:
- * The Cry gene family from Bacillus thuringiensis encodes proteins with specific insecticidal activity.
- * Cry proteins are crucial for pest control, with research focusing on their structure-function relationships and target specificity.
- * Specific residues and domains are known to be vital for Cry protein interaction with insect receptors.
Purpose of the Study:
- * To investigate adaptive evolution in Cry proteins using a maximum likelihood method.
- * To identify specific amino acid residues under positive selection.
- * To correlate identified residues with insect specificity determination and functional divergence.
Main Methods:
- * Maximum likelihood analysis to detect positive selection in Cry protein sequences.
- * Integration of existing mutagenesis data.
- * Comparative analysis of identified positively selected sites with known functional domains.
Main Results:
- * Identification of 24 residues under positive selection in Cry proteins.
- * All identified residues are located within Domain II or Domain III.
- * These residues are strongly implicated in determining insect specificity.
Conclusions:
- * Adaptive evolution, particularly positive selection, plays a significant role in Cry protein diversification.
- * The identified residues are critical for insect specificity and may be driven by an evolutionary "arms race" with insects.
- * These positively selected sites offer valuable targets for future structural and functional studies of Cry proteins.
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