Cloning and characterization of two novel crystal protein genes from a Bacillus thuringiensis serovar dakota strain

Two genes encoding the 32- and 40-kDa polypeptides of Bacillus thuringiensis strain 90-F-45-14 crystals were cloned, expressed in an acrystalliferous B. thuringiensis strain, and sequenced. The polypeptides had deduced molecular weights of 30,319 and 33,885, respectively. The amino acid sequence of...

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Bibliographic Details
Published in:Current microbiology 2003-01, Vol.46 (1), p.33-38
Main Authors: Kim, Ho San, Saitoh, Hiroyuki, Yamashita, Satoko, Akao, Tetsuyuki, Park, Yu Shin, Maeda, Minoru, Tanaka, Rie, Mizuki, Eiichi, Ohba, Michio
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Bacillus thuringiensis
Bacillus thuringiensis - cytology
Bacillus thuringiensis - genetics
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - isolation & purification
Bacterial Toxins
Bacteriology
Base Sequence
Cloning
Cloning, Molecular
Crystallization
Crystals
Electrophoresis, Polyacrylamide Gel
Endotoxins - chemistry
Endotoxins - genetics
Endotoxins - isolation & purification
Gene Expression Regulation, Bacterial
Genes
Genes, Bacterial
Hemolysin Proteins
Microbiology
Models, Genetic
Polypeptides
Proteins
Spores, Bacterial - ultrastructure
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Summary:Two genes encoding the 32- and 40-kDa polypeptides of Bacillus thuringiensis strain 90-F-45-14 crystals were cloned, expressed in an acrystalliferous B. thuringiensis strain, and sequenced. The polypeptides had deduced molecular weights of 30,319 and 33,885, respectively. The amino acid sequence of the 32-kDa protein was 37.7% identical to the known sequence of a non-insecticidal parasporal protein in B. thuringiensis serovar thompsoni crystals. The sequence of the cloned 40-kDa protein was 37.0% and 22.3% identical to that of the existing Cry protein classes, Cry15Aa1 and Cry23Aa1, respectively. Thus, this protein constitutes a novel protein class, Cry33Aa1. The open reading frames of the two genes were located on the predominant plasmid of 17,629 bp (=11,752 MDa) in the same orientation, and they were separated by the sequence of 32 nucleotides. The two proteins are likely produced simultaneously from a single transcript to form spherical crystals.
ISSN:0343-8651
1432-0991
DOI:10.1007/s00284-002-3801-y