Expression in Escherichia coli of a cloned crystal protein gene of Bacillus thuringiensis subsp. israelensis | Zendy

Kent M. McLean | Zendy; H.R. Whiteley | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

Expression in Escherichia coli of a cloned crystal protein gene of Bacillus thuringiensis subsp. israelensis

Author(s) -

Kent M. McLean,

H.R. Whiteley

Publication year - 1987

Publication title -

journal of bacteriology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.652

H-Index - 246

eISSN - 1067-8832

pISSN - 0021-9193

DOI - 10.1128/jb.169.3.1017-1023.1987

Subject(s) - biology , bacillus thuringiensis , escherichia coli , recombinant dna , plasmid , microbiology and biotechnology , gene , dna , bacillaceae , molecular cloning , peptide sequence , bacteria , bacillus subtilis , biochemistry , genetics

A ca. 10-kilobase (kb) HindIII fragment of plasmid DNA from Bacillus thuringiensis subsp. israelensis was cloned into plasmid pUC9 and transformed into Escherichia coli. Extracts of the recombinant strain contained a 27-kilodalton (kDa) peptide that reacted with antibodies to a 27-kDa peptide isolated from crystals produced by B. thuringiensis subsp. israelensis. Extracts of the recombinant strain were hemolytic and toxic to Aedes aegypti larvae. Full expression of the 27-kDa peptide required the presence of a ca. 0.8-kb region of DNA located 4 kb upstream from the structural gene; the 0.8-kb region could be present in cis or trans relative to the gene and apparently acted post-transcriptionally. Analysis of maxicells showed that the 10-kb insert also coded for peptides of 67, 20, and 16 kDa; data obtained with different subclones suggest that the 20-kDa peptide is encoded in the 0.8-kb DNA region.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research