Formation of crystals of the insecticidal proteins of Bacillus thuringiensis subsp. aizawai IPL7 in Escherichia coli.
Escherichia coli JM103 cells harboring expression plasmid pTB1 or pKC6 synthesized the 130- and 135-kilodalton insecticidal proteins, respectively, of Bacillus thuringiensis subsp. aizawai IPL7, and both products accumulated as cytoplasmic inclusion bodies. Amorphous inclusions which contained contaminating proteins, together with the corresponding insecticidal proteins, were formed in cultures at 37 degrees C, but bipyramidal crystals practically free of contaminants were observed at 30 degrees C. Although 9.8% of the amino acids were substituted between these two proteins, both protein crystals had the same shape as those of the parental B. thuringiensis strain, which produced both proteins.
Oeda
K
K
Biotechnology Laboratory, Takarazuka Research Center, Sumitomo Chemical Company, Hyogo, Japan.
Inouye
K
K
Ibuchi
Y
Y
Oshie
K
K
Shimizu
M
M
Nakamura
K
K
Nishioka
R
R
Takada
Y
Y
Ohkawa
H
H
D001413:Bacillus thuringiensis; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D003001:Cloning, Molecular; D003460:Crystallization; D004731:Endotoxins; D004926:Escherichia coli / Q000235:genetics / Q000648:ultrastructure; D006460:Hemolysin Proteins; D008854:Microscopy, Electron; D010572:Pest Control, Biological; D011994:Recombinant Proteins
D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011994:Recombinant Proteins; C030956:insecticidal crystal protein, Bacillus Thuringiensis