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

P. A. Koni, D. J. Ellar

Research output: Contribution to journalArticlepeer-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 languageEnglish (US)
Pages (from-to)319-327
Number of pages9
JournalJournal of Molecular Biology
Volume229
Issue number2
DOIs
StatePublished - Jan 20 1993
Externally publishedYes

Keywords

  • Bacillus thuringiensis
  • Cloning
  • Expression
  • Sequence
  • Δ-endotoxin

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

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