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dc.contributor.authorSiriya Thammachaten_US
dc.contributor.authorNuanwan Pungtanomen_US
dc.contributor.authorSomruathai Kidsanguanen_US
dc.contributor.authorWanwarang Pathaichindachoteen_US
dc.contributor.authorBoonhiang Promdonkoyen_US
dc.contributor.authorChartchai Krittanaien_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherThailand National Center for Genetic Engineering and Biotechnologyen_US
dc.identifier.citationBMB Reports. Vol.43, No.6 (2010), 427-431en_US
dc.description.abstractCyt2Aa2 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.en_US
dc.rightsMahidol Universityen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleAmino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxinen_US
Appears in Collections:Scopus 2006-2010

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