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  • 1985-1989  (2)
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Material
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  • 1
    Electronic Resource
    Electronic Resource
    Cloning and expression of an entomocidal protein gene from Bacillus thuringiensis galleriae toxic to both lepidoptera and diptera (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 59 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A gene encoding a 61 kDa entomocidal (P2) protein from Bacillus thuringiensis galleriae was cloned in Escherichia coli using oligonucleotide probes corresponding to N- and C-terminal DNA sequences of a Kurstaki P2 gene. When the gene of a 5.8 kb HindIII fragment was transformed into B. subtilis on a shuttle vector, sporulation was completely inhibited and expression could not be detected. When B. megaterium was transformed with the same plasmid, only 10% of the cells sporulated and a 61 kDa P2 protein which cross-reacted with kurstaki P2 antiserum was synthesised. Cell lysates of the transformed B. megaterium were found to be toxic to both lepidopteran and dipteran larvae.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03109.x
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Delineation of the toxin coding fragments and an insect-specificity region of a dual toxicity Bacillus thuringiensis crystal protein gene (1989)
    Oxford, UK : Blackwell Publishing Ltd
    FEMS microbiology letters 58 (1989), S. 0 
    Details
    ISSN: 1574-6968
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: Abstract A series of deletion mutants have been constructed from the dual toxicity Bacillus thuringiensis aizawai IC1 (Bta IC1) crystal protein gene. The mutant toxin genes were expressed in Escherichia coli, their protein products purified and the authenticity of these mutant proteins confirmed immunologically. Analysis of the toxicity spectra of these mutants revealed that lepidopteran toxicity is located on the N-terminal region of the toxin between residues Ile30-Glu595. 3′ deletion of a further 37 residues from Glu595 of the lepidopteran-specific toxin abolished lepidopteran toxicity but the resulting protein consisting of residues Ile30-Gly558 was still fully toxic to dipteran larvae and cells. Another mutant crystal protein gene truncated to encode residues between Ile30-Gly563 was toxic only to diptera. These data indicate that the determinants of lepidopteran specificity in the Bta IC1 toxin are located between residues Gly558-Glu595 and that the N-terminal portion of the toxin between Ile30-Gly558 is sufficient to express dipteran toxicity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1574-6968.1989.tb03037.x
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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