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Cloning and characterization of the crystal protein-encoding gene of Bacillus thuringiensis subsp. yunnanensis.

ABSTRACT: Molecular cloning and characterization of a novel cry gene, cry32Aa, of Bacillus thuringiensis subsp. yunnanensis was carried out. The Cry32Aa protein was predicted to have a molecular mass of 139.2 kDa and was found to have an unusual 42-amino-acid-long tail at the C terminus. The cry32Aa gene was localized on the 103-MDa plasmid of the organism. Bioassays showed no toxicity against several moths and mosquitoes. However, it exhibited weak toxicity against larvae of the diamondback moth, Plutella xylostella.

SUBMITTER: Balasubramanian P

PROVIDER: S-EPMC126593 | biostudies-literature | 2002 Jan

REPOSITORIES: biostudies-literature

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Cloning and characterization of the crystal protein-encoding gene of Bacillus thuringiensis subsp. yunnanensis.

Balasubramanian Periasamy P Jayakumar R R Shambharkar Prashant P Unnamalai N N Pandian S Karutha SK Kumaraswami N Selvamuthu NS Ilangovan R R Sekar Vaithilingam V

Applied and environmental microbiology 20020101 1

Molecular cloning and characterization of a novel cry gene, cry32Aa, of Bacillus thuringiensis subsp. yunnanensis was carried out. The Cry32Aa protein was predicted to have a molecular mass of 139.2 kDa and was found to have an unusual 42-amino-acid-long tail at the C terminus. The cry32Aa gene was localized on the 103-MDa plasmid of the organism. Bioassays showed no toxicity against several moths and mosquitoes. However, it exhibited weak toxicity against larvae of the diamondback moth, Plutell ...[more]

PMID: 11772653

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