Crystal structure of Cry51Aa1: A potential novel insecticidal aerolysin-type β-pore-forming toxin from Bacillus thuringiensis
نویسندگان
چکیده
منابع مشابه
Membrane pore architecture of a cytolytic toxin from Bacillus thuringiensis.
To investigate the membrane pore structure of Cyt2Aa1 toxin from Bacillus thuringiensis, 14 single-cysteine substitutions of the toxin were constructed. Five of these mutants (L172C, V186C, L189C, E214C and L220C) yielded characteristic products when processed by proteinase K; other mutants were degraded by this enzyme. Mutants that yielded characteristic proteolysed products and wild-type toxi...
متن کاملThe Aerolysin-Like Toxin Family of Cytolytic, Pore-Forming Toxins
Pore-forming toxins (PFTs) represent the largest known group of bacterial protein toxins to date. Membrane insertion and subsequent pore-formation occurs after initial binding to cell-surface receptor and oligomerization. Aerolysin, a toxin produced by the Gram-negative bacterium Aeromonas hydrophila and related species, belongs to the PFT group and shares a common mechanism of action involving...
متن کاملIsolation and characterization of a novel insecticidal crystal protein gene from Bacillus thuringiensis subsp. aizawai.
Bacillus thuringiensis subsp. aizawai EG6346, a novel grain dust isolate, was analyzed by Southern blot hybridization for its insecticidal crystal protein (ICP) gene profile. Strain EG6346 lacks previously characterized cryIA ICP genes yet does possess novel cryI-related gene sequences. A recombinant genomic plasmid library was constructed for strain EG6346 in Escherichia coli. One recombinant ...
متن کاملThe Bacillus thuringiensis insecticidal toxin binds biotin-containing proteins.
Brush border membrane vesicles from larvae of the tobacco hornworm, Manduca sexta, contain protein bands of 85 and 120 kDa which react directly with streptavidin conjugated to alkaline phosphatase. The binding could be prevented either by including 10 microM biotin in the reaction mixture or by prior incubation of the brush border membrane vesicles with an activated 60- to 65-kDa toxin from Bac...
متن کاملAnalysis of mutations in the pore-forming region essential for insecticidal activity of a Bacillus thuringiensis delta-endotoxin.
The Bacillus thuringiensis insecticidal delta-endotoxins have a three-domain structure, with the seven amphipathic helices which comprise domain I being essential for toxicity. To better define the function of these helices in membrane insertion and toxicity, either site-directed or random mutagenesis of two regions was performed. Thirty-nucleotide segments in the B. thuringiensis cry1Ac1 gene,...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical and Biophysical Research Communications
سال: 2015
ISSN: 0006-291X
DOI: 10.1016/j.bbrc.2015.04.068