| Autor: |
Chartchai Krittanai, Siriya Thammachat, Boonhiang Promdonkoy, Wanwarang Pathaichindachote, Somruathai Kidsanguan, Nuanwan Pungtanom |
| Rok vydání: |
2010 |
| Předmět: |
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| Zdroj: |
BMB Reports. 43:427-431 |
| ISSN: |
1976-6696 |
| Popis: |
Cyt2Aa2 is a mosquito-larvicidal protein produced as a 29 kDa crystalline protoxin from Bacillus thuringiensis subsp. darmstadiensis. To become an active toxin, proteolytic processing is required to remove amino acids from its N- and C-termini. This study aims to investigate the functional role of amino acid residues on the N-terminal Beta1 and C-terminal alphaF of Cyt2Aa2 protoxin. Mutant protoxins were constructed, characterized and compared to the wild type Cyt2Aa2. Protein expression data and SDS-PAGE analysis revealed that substitution at leucine- 33 (L33) of Beta1 has a critical effect on dimer formation and structural stability against proteases. In addition, amino acids N230 and I233-F237 around the C-terminus alphaF demonstrated a crucial role in protecting the protoxin from proteolytic digestion. These results suggested that Beta1 and alphaF on the Nand C-terminal ends of Cyt2Aa2 protoxin play an important role in the molecular interaction and in maintaining the structural stability of the protoxin. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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