Characterized full-length and truncated plasmid clones of the crystal protein of Bacillus thuringiensis subsp. kurstaki HD-73 and their toxicity to Manduca sexta
作者： Michael J. Adang , Michael J. Staver , Thomas A. Rocheleau , Jacqui Leighton , Richard F. Barker
DOI: 10.1016/0378-1119(85)90184-2
关键词: Bacillus thuringiensis 、 Protein primary structure 、 Plasmid 、 Gene product 、 Coding region 、 Nucleic acid sequence 、 Molecular biology 、 Biology 、 Escherichia coli 、 Gene
摘要: Abstract Bacillus thuringiensis subsp. kurstaki HD-73 produces a crystal protein which is lethal to many lepidopteran larvae. The gene encoding this has been isolated from 75-kb plasmid and engineered into recombinant Escherichia coli for analysis. complete nucleotide sequences of the coding region 387-bp 5' 376-bp 3' have determined. 3537-bp specify M r 133330. full-length several 3'-truncated derivatives were examined in both E. an minicell-expression system determine if carboxy end essential toxicity. results presented here provide primary structure show that N-terminal 68-kDal peptide toxic, but at lower level than product.
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