Cloning and characterization of a novel Bacillus thuringiensis cytolytic delta-endotoxin

Pandelakis Koni; D. J. Ellar

doi:10.1006/jmbi.1993.1037

Cloning and characterization of a novel Bacillus thuringiensis cytolytic delta-endotoxin

Pandelakis Koni, D. J. Ellar

Infectious Disease

Research output: Contribution to journal › Article › peer-review

63 Scopus citations

Abstract

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 sequence 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.

Original language	English (US)
Pages (from-to)	319-327
Number of pages	9
Journal	Journal of Molecular Biology
Volume	229
Issue number	2
DOIs	https://doi.org/10.1006/jmbi.1993.1037
State	Published - Jan 20 1993

Keywords

Bacillus thuringiensis
Cloning
Expression
Sequence
Δ-endotoxin

ASJC Scopus subject areas

Molecular Biology

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10.1006/jmbi.1993.1037

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abstract = "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 sequence 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.",

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N2 - 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 sequence 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.

AB - 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 sequence 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.

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Cloning and characterization of a novel Bacillus thuringiensis cytolytic delta-endotoxin

Abstract

Keywords

ASJC Scopus subject areas

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