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Please use this identifier to cite or link to this item: http://repository.li.mahidol.ac.th/dspace/handle/123456789/28824
Title: Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
Authors: Siriya Thammachat
Nuanwan Pungtanom
Somruathai Kidsanguan
Wanwarang Pathaichindachote
Boonhiang Promdonkoy
Chartchai Krittanai
Mahidol University
Thailand National Center for Genetic Engineering and Biotechnology
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Jan-2010
Citation: BMB Reports. Vol.43, No.6 (2010), 427-431
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.
URI: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=77955785259&origin=inward
http://repository.li.mahidol.ac.th/dspace/handle/123456789/28824
ISSN: 1976670X
19766696
Appears in Collections:Scopus 2006-2010

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