Isoleucine at position 150 of Cyt2Aa toxin from Bacillus thuringiensis plays an important role during membrane binding and oligomerization
| Autor: | Chartchai Krittanai, Wanwarang Pathaichindachote, Amporn Rungrod, Sumarin Soonsanga, Boonhiang Promdonkoy, Mongkon Audtho |
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| Rok vydání: | 2013 |
| Předmět: |
Membrane binding
medicine.medical_treatment Mutant Bacillus thuringiensis Plasma protein binding Biology Calorimetry medicine.disease_cause Biochemistry lcsh:Biochemistry Hemolysin Proteins Biopolymers Bacterial Proteins medicine Cyt toxin Oligomerization lcsh:QD415-436 Isoleucine Molecular Biology lcsh:QH301-705.5 Research Articles DNA Primers Alanine chemistry.chemical_classification Protease Bacillus thuringiensis Toxins Base Sequence Toxin Wild type General Medicine Amino acid Endotoxins chemistry lcsh:Biology (General) Mutagenesis Protein Binding |
| Zdroj: | BMB Reports BMB Reports, Vol 46, Iss 3, Pp 175-180 (2013) |
| ISSN: | 1976-670X |
| Popis: | Cyt2Aa2 is a mosquito larvicidal and cytolytic toxin produced by Bacillus thuringiensis subsp. darmstadiensis. The toxin becomes inactive when isoleucine at position 150 was replaced by alanine. To investigate the functional role of this position, Ile150 was substituted with Leu, Phe, Glu and Lys. All mutant proteins were produced at high level, solubilized in carbonate buffer and yielded protease activated product similar to those of the wild type. Intrinsic fluorescence spectra analysis suggested that these mutants retain similar folding to the wild type. However, mosquito larvicidal and hemolytic activities dramatically decreased for the I150K and were completely abolished for I150A and I150F mutants. Membrane binding and oligomerization assays demonstrated that only I150E and I150L could bind and form oligomers on lipid membrane similar to that of the wild type. Our results suggest that amino acid at position 150 plays an important role during membrane binding and oligomerization of Cyt2Aa2 toxin. [BMB Reports 2013; 46(3): 175-180] |
| Databáze: | OpenAIRE |
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