Cloning and Characterization of a Novel Bacillus thuringiensis Cytolytic Delta-Endotoxin

A gene encoding a major entomocidal polypeptide from Bacillus thuringiensis subspecies kyushuensis δ-endotoxin crystals (CytB) was cloned into Escherichia coli and sequenced. The deduced amino acid sequence gave a predicted molecular mass of 29 236 Da and showed 39% identity and 70% similarity with...

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Veröffentlicht in:	Journal of molecular biology 1993-01, Vol.229 (2), p.319-327
Hauptverfasser:	Koni, P.A., Ellar, D.J.
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacillus thuringiensis Bacillus thuringiensis - genetics Bacterial Proteins Bacterial Toxins Base Sequence Biological and medical sciences cloning Cloning, Molecular DNA, Bacterial Endotoxins - genetics Endotoxins - metabolism Escherichia coli expression Fundamental and applied biological sciences. Psychology Genes. Genome Hemolysin Proteins Insecticides - metabolism Microscopy, Electron Molecular and cellular biology Molecular genetics Molecular Sequence Data Restriction Mapping sequence Sequence Homology, Amino Acid δ-endotoxin
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Beschreibung
Zusammenfassung:	A gene encoding a major entomocidal polypeptide from Bacillus thuringiensis subspecies kyushuensis δ-endotoxin crystals (CytB) was cloned into Escherichia coli and sequenced. The deduced amino acid sequence gave a predicted molecular mass of 29 236 Da and showed 39% identity and 70% similarity with the 27,371 Da CytA protein from Bacillus thuringiensis subspecies israelensis. The larger size of CytB compared to CytA appears to be due to additional sequences in CytB after the CytA C-terminus. Unlike CytA, CytB was freely expressed in Escherichia coli and formed cytoplasmic inclusions without the need for a "helper" protein. Electron microscopic observation of CytB inclusions revealed them to be generally amorphous, but examples possessing some lattice structure were seen.
ISSN:	0022-2836 1089-8638
DOI:	10.1006/jmbi.1993.1037