Activation of a cryptic crystal protein gene of Bacillus thuringiensis subspecies kurstaki by gene fusion and determination of the crystal protein insecticidal specificity.
DNA hybridization with the insecticidal crystal protein gene cryllA (formerly cryBl) of Bacillus thuringiensis supspecies kurstaki has shown that subspecies kurstaki contains a cryllA-related sequence in addition to the cryllA gene (Donovan et al., 1988a). We have cloned the cryllA-related sequence and have determined that the sequence, which has been designated cryllB, is 89% identical to the cryllA gene. Recombinant B. thuringiensis cells harbouring the cloned cryllB gene produced very little CryllB protein. A high level of production of the CryllB protein was achieved by fusing the regulatory region of the crylllA crystal protein gene to the cryllB gene. The CryllB protein was found to be highly toxic to Lymantria dispar, Heliothis virescens and Trichoplusia ni, and was not toxic to Aedes aegypti.
Dankocsik
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Ecogen Inc., Langhorne, Pennysylvania 19047.
Donovan
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Jany
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D000595:Amino Acid Sequence; D000818:Animals; D001413:Bacillus thuringiensis / Q000235:genetics*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000235:genetics* / Q000494:pharmacology; D001427:Bacterial Toxins; D001483:Base Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial; D004731:Endotoxins; D015870:Gene Expression; D005798:Genes, Bacterial; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D012045:Regulatory Sequences, Nucleic Acid; D015183:Restriction Mapping; D012689:Sequence Homology, Nucleic Acid
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004269:DNA, Bacterial; D004731:Endotoxins; D006460:Hemolysin Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis