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Title: Isoleucine at position 150 of Cyt2Aa toxin from Bacillus thuringiensis plays an important role during membrane binding and oligomerization
Authors: Wanwarang Pathaichindachote
Amporn Rungrod
Mongkon Audtho
Sumarin Soonsanga
Chartchai Krittanai
Boonhiang Promdonkoy
Thailand National Center for Genetic Engineering and Biotechnology
Mahidol University
Keywords: Biochemistry, Genetics and Molecular Biology
Issue Date: 1-Mar-2013
Citation: BMB Reports. Vol.46, No.3 (2013), 175-180
Abstract: Cyt2Aa2 is a mosquito larvicidal and cytolytic toxin produced by Bacillus thuringiensis subsp. darmstadiensis. The toxin becomes inactive when isoleucine at position 150 was replaced by alanine. To investigate the functional role of this position, Ile150 was substituted with Leu, Phe, Glu and Lys. All mutant proteins were produced at high level, solubilized in carbonate buffer and yielded protease activated product similar to those of the wild type. Intrinsic fluorescence spectra analysis suggested that these mutants retain similar folding to the wild type. However, mosquito larvicidal and hemolytic activities dramatically decreased for the I150K and were completely abolished for I150A and I150F mutants. Membrane binding and oligomerization assays demonstrated that only I150E and I150L could bind and form oligomers on lipid membrane similar to that of the wild type. Our results suggest that amino acid at position 150 plays an important role during membrane binding and oligomerization of Cyt2Aa2 toxin. © 2013 by the The Korean Society for Biochemistry and Molecular Biology.
ISSN: 1976670X
Appears in Collections:Scopus 2011-2015

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