Effects of Bacillus thuringiensis var. israelensis 20-kDa Protein on Production of the Bti 130-kDa Crystal Protein in Escherichia coli

• Published in: Bioscience, biotechnology, and biochemistry Vol. 56; no. 9; pp. 1429 - 1433
• Main Authors: Yoshisue, Hajime, Yoshida, Ken-ichi, Sen, Kikuo, Sakai, Hiroshi, Komano, Tohru
• Format: Journal Article
• Language: English
• Published: Tokyo Taylor & Francis 1992; Japan Society for Bioscience Biotechnology and Agrochemistry
• Subjects: Amino Acid Sequence; Bacillus thuringiensis - genetics; Bacillus thuringiensis - metabolism; Bacterial Proteins - biosynthesis; Bacterial Proteins - genetics; Bacterial Proteins - pharmacology; Bacterial Toxins; Base Sequence; Biological and medical sciences; Biotechnology; Cloning, Molecular; Endotoxins; Escherichia coli - genetics; Escherichia coli - metabolism; Fundamental and applied biological sciences. Psychology; Genes, Bacterial - physiology; Genetic engineering; Genetic technics; Hemolysin Proteins; Methods. Procedures. Technologies; Modification of gene expression level; Molecular Sequence Data; Bacillus thuringiensis var. israelensis; Plasmid; Bacillales; Escherichia coli; Blotting assay; Bacteria; Stimulation; Recombinant protein; Bacillaceae; Gene expression; Enterobacteriaceae
• ISSN: 0916-8451; 1347-6947
• DOI: 10.1271/bbb.56.1429

A 20-kDa protein of Bacillus thuringiensis var. israelensis (Bti) has been shown to be necessary for the efficient expression of the 27-kDa mosquitocidal protein gene in Escherichia coli. We have investigated the effects of this 20-kDa protein on the expression of two 130-kDa mosquitocidal protein genes (cryIVA, cryIVB) in E. coli by supplying the 20-kDa protein gene in trans. When a recombinant plasmid, pLH4BX, which was constructed to express cryIVA under the E. coli lac promoter on pUC19, coexisted with the 20-kDa protein gene, a striking increase in production of the fused CryIVA was detected. This was not accompanied by an increase in the amount of intracellular mRNA, suggesting that 20-kDa protein exerts a posttranscriptional effect. We conclude that the 20-kDa protein also stimulates the production of 130-kDa protein in E. coli.