Two highly related insecticidal crystal proteins of Bacillus thuringiensis subsp. kurstaki possess different host range specificities
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ArticleLanguage: En Publication details: 1989ISSN: - 0021-9193
- 89-109178
| Item type | Current library | Collection | Call number | Copy number | Status | Date due | Barcode | Item holds | |
|---|---|---|---|---|---|---|---|---|---|
| Article | CIMMYT Knowledge Center: John Woolston Library | AGRIS Collection | 89-109178 (Browse shelf(Opens below)) | 1 | Available | 89-109178 |
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Two genes encoding insecticidal crystal proteins from Bacillus thuringiensis subsp. kurstaki HD-1 were cloned and sequenced. Both genes, designated cryB1, and cryB2, encoded polypeptides of 633 amino acids having a molecular mass of ca. 71 kilodaltons (kDa). Despite the fact that these two proteins display 87 identity in amino acid sequence, they exhibit different toxin specificities. The cryB1 gene product is toxic to both dipteran (Aedes aegypti) and lepidopteran (Manduca sexta) larvae, whereas the cryB2 gene product is toxic only to the latter. DNA sequence analysis indicates that cryB1 is the distal gene of an operon which is comprised of three
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