Functional Analysis of Two Processed Fragments of Bacillus thuringiensis Cry11A Toxin

DOI Web Site Web Site PubMed 2 Citations 17 References

Bibliographic Information

Other Title
  • Functional Analysis of Two Processed Fragments of<i>Bacillus thuringiensis</i>Cry11A Toxin

Search this article

Abstract

The 70-kDa protoxin of Cry11A, a dipteran-specific insecticidal protein, was processed by trypsin into 36- and 32-kDa fragments. To investigate the potent function of the two processed fragments, a GST (Glutathione-S-transferase) fusion protein of each polypeptide was constructed. While neither the 36- nor the 32-kDa fragment was toxic to Culex pipiens larvae, coexpression of the two fragments restored the insecticidal activity. Furthermore, the coprecipitation experiment demonstrated that the 36-kDa fragment was associated with the 32-kDa fragment. It was, therefore, shown that the coexistence of the two processed fragments of Cry11A was essential for the toxicity. The mutant of the 36-kDa fragment lacking the region from Gly257 to Arg360 bound to the 32-kDa fragment but the coexpression with the 32-kDa fragment resulted in no toxicity, suggesting that this region was involved in insecticidal activity.

Journal

Citations (2)*help

See more

References(17)*help

See more

Keywords

Details 詳細情報について

Report a problem

Back to top