Publication: Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
Issued Date
2010-01-01
Resource Type
ISSN
1976670X
19766696
19766696
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2-s2.0-77955785259
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Mahidol University
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SCOPUS
Bibliographic Citation
BMB Reports. Vol.43, No.6 (2010), 427-431
Suggested Citation
Siriya Thammachat, Nuanwan Pungtanom, Somruathai Kidsanguan, Wanwarang Pathaichindachote, Boonhiang Promdonkoy, Chartchai Krittanai Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin. BMB Reports. Vol.43, No.6 (2010), 427-431. doi:10.5483/BMBRep.2010.43.6.427 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/28824
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Title
Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
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Abstract
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 N- and C-terminal ends of Cyt2Aa2 protoxin play an important role in the molecular interaction and in maintaining the structural stability of the protoxin.