Involvement of a possible chaperonin in the efficient expression of a cloned CryIIA delta-endotoxin gene in Bacillus thuringiensis.
The Bacillus thuringiensis cryIIA delta-endotoxin gene is found as the third-gene in a three-gene operon, with a sporulation-dependent promoter lying upstream of the first gene, orf1. We show here that the polypeptide product of the middle gene (orf2) is required for efficient expression of the toxin gene. In the absence of a functional ORF2 polypeptide the toxin does not form the crystalline inclusions characteristic of other known Bacillus thuringiensis toxins. We discuss the importance of this finding with respect to the possible role of chaperonins in the crystallization of these proteins.
Department of Biochemistry, University of Cambridge, UK.
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N
Crickmore
D J
DJ
Ellar
D000595:Amino Acid Sequence; D001413:Bacillus thuringiensis / Q000235:genetics* / Q000378:metabolism; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D001483:Base Sequence; D018833:Chaperonins; D003001:Cloning, Molecular; D004731:Endotoxins / Q000096:biosynthesis*; D015870:Gene Expression / Q000502:physiology*; D005798:Genes, Bacterial / Q000502:physiology*; D006460:Hemolysin Proteins; D008969:Molecular Sequence Data; D011506:Proteins / Q000502:physiology*
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011506:Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D018833:Chaperonins