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KMID : 0624620100430060427
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BMB Reports
2010 Volume.43 No. 6 p.427 ~ p.431
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Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
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Thammachat Siriya
Pungtanom Nuanwan
Kidsanguan Somruathai
Pathaichindachote Wanwarang
Promdonkoy Boonhiang
Krittanai Chartchai
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Abstract
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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 β1 and C-terminal αF 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 β1 has a critical effect on dimer formation and structural stability against proteases. In addition, amino acids N230 and I233-F237 around the C-terminus αF demonstrated a crucial role in protecting the protoxin from proteolytic digestion. These results suggested that β1 and αF 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.
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KEYWORD
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Bacillus thuringiensis, Cytolytic toxin, Mutagenesis, Protein folding, Toxicity
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