Abstract
The Cry8Ea1 protoxin is a DNA-protein complex. Both forms of the Cry8Ea1 toxin (with or without DNA binding) were obtained separately, and their stability and ability to insert into a phospholipid monolayer in vitro were compared. The presence of DNA can prevent the toxin from aggregation. Data regarding the penetration of the Cry8Ea1 toxin and Cry8Ea1 toxin-DNA complex into the air/water interface without a phospholipid monolayer show that the Cry8Ea1 toxin-DNA complex is more likely to move towards the air/water interface and is more hydrophobic. Experiments examining the protein interaction with the phospholipid monolayer show that the ability of the Cry8Ea1 toxin-DNA complex to insert into the lipid bilayer is much greater than that of the Cry8Ea1 toxin without DNA.
Original language | English |
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Pages (from-to) | 203-210 |
Number of pages | 8 |
Journal | FEMS Microbiology Letters |
Volume | 317 |
Issue number | 2 |
DOIs | |
Publication status | Published - Apr 2011 |
Keywords
- Aggregation
- Bacillus thuringiensis
- Protoxin-DNA
- Toxin-DNA
- δ-endotoxin