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Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
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Document Title
Amino acid substitution on β1 and αF of Cyt2Aa2 affects molecular interaction of protoxin
Author
Thammachat S., Pungtanom N., Kidsanguan S., Pathaichindachote W., Promdonkoy B., Krittanai C.
Name from Authors Collection
Affiliations
Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Phuttamonthon 4 Road, Salaya, Nakhon Pathom 73170, Thailand; National Center for Genetic Engineering and Biotechnology, National Science and Technology Development Agency, 113 Phaholyothin Road, Klong 1, Klong Luang, Pathum Thani 12120, Thailand
Type
Article
Source Title
BMB Reports
ISSN
19766696
Year
2010
Volume
43
Issue
6
Page
427-431
Open Access
Gold
Publisher
The Biochemical Society of the Republic of Korea
DOI
10.5483/BMBRep.2010.43.6.427
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.
Keyword
Bacillus thuringiensis | Cytolytic toxin | Mutagenesis | Protein folding | Toxicity
Industrial Classification
Knowledge Taxonomy Level 1
Knowledge Taxonomy Level 2
Knowledge Taxonomy Level 3
License
Public Nuri
Rights
Korea Institute of Science and Technology Information https://www.kisti.re.kr/pageView/521?t=1648956401355
Publication Source
Scopus