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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]

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