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Expression of the Full-Length and 3′-Spliced cry 1Ab Gene in the 135-kDa Crystal Protein Minus Derivative of Bacillus thuringiensis subsp. kyushuensis

Yu, J., Xie, R., Tan, L., Xu, W., Zeng, S., Chen, J., Tang, M. and Pang, Y. (2002) Expression of the Full-Length and 3′-Spliced cry 1Ab Gene in the 135-kDa Crystal Protein Minus Derivative of Bacillus thuringiensis subsp. kyushuensis. Current Microbiology, 45 (2). pp. 133-138.

Link to Published Version: https://doi.org/10.1007/s00284-001-0092-7
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Abstract

Bacillus thuringiensis produces a 130 –135-kDa insecticidal protein in the form of bipyramidal crystal which is toxic to lepidopteran larvae. Part of the C-terminal region of the native Cry1Ab was replaced by a heterologous sequence of Cry11Aa C-terminus to get a 3 -spliced cry 1Ab gene. The full-length cry 1Ab and 3 -spliced cry 1Ab, which were both cloned into the E. coli–B. thuringiensis shuttle expression vector pHZB1, were expressed in a 135-kDa crystal protein minus derivative of B. thuringiensis subsp. kyushuensis (4U1-Cry 135 ). The crystal shape of Cry1Ab proteins from both recombinants was regularly bipyramidal, while the crystal size of the intact Cry1Ab was approximately fivefold larger than the 3 -spliced Cry1Ab. In addition, these two kinds of Cry1Ab proteins had similar toxicity against Argyrogramma agnata larvae.

Publication Type: Journal Article
Publisher: Springer Verlag
Copyright: © 2002 Springer-Verlag New York Inc.
URI: http://researchrepository.murdoch.edu.au/id/eprint/37548
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