Analysis of 66 kDa toxin from Bacillus thuringiensis subsp. kurstaki reveals differential amino terminal processing of protoxin by endogenous protease(s).
The endogenous protease(s) activated crystal toxin from Bacillus thuringiensis subsp. kurstaki was purified and examined. The purified toxin was homogenous, as demonstrated by two-dimensional polyacrylamide gel electrophoresis and contained 1.38 mumoles neutral sugar and 9 nmoles sialic acid per mg protein amino terminal amino acid sequence data revealed that the toxin is a cleavage product of 132 kDa protoxin with glutamic acid-30 of the deduced amino acid sequence of the crystal protein (Schnepf, H.E., Wong, H.C. and Whiteley, H.R. (1985) J. Biol. Chem. 260: 6264-6272) at the amino terminus.
Kumar
N S
NS
Department of Biochemistry, Osmania University, Hyderabad, India.
Venkateswerlu
G
G
D000595:Amino Acid Sequence; D000818:Animals; D001413:Bacillus thuringiensis / Q000378:metabolism*; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism* / Q000633:toxicity; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism*; D010450:Endopeptidases / Q000378:metabolism*; D004731:Endotoxins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism* / Q000633:toxicity; D006460:Hemolysin Proteins; D008970:Molecular Weight; D011498:Protein Precursors / Q000737:chemistry* / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D018411:Spodoptera
D000083722:Bacillus thuringiensis Toxins; C029103:Bacillus thuringiensis protoxin; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D011498:Protein Precursors; C030956:insecticidal crystal protein, Bacillus Thuringiensis; D010450:Endopeptidases