[Effect of quorum sensing response regulator nprR deletion on expression of cry protein in Bacillus thuringiensis]

Wei Sheng Wu Xue Bao. 2010 Nov;50(11):1550-5.
[Article in Chinese]

Abstract

Objective: The role of Quroum Sensing response regulator nprR on the expression of Cry protein in B. thuringiensis HD-73 was studied.

Methods: The nprR gene deletion mutant HD73 (delta nprR) was constructed by using of homologous recombination. Beta-galactosidase assay of cry1Ac'-lacZ gene fusion and SDS-PAGE in both HD-73 and HD73 (delta nprR) strains were performed to analyze the effect of nprR gene deletion on expression of cry1lAc gene.

Results: Beta-galactosidase assay of nprR'-lacZ in both LB and Schaeffer' s sporulation medium showed nprR gene in B. thuringiensis was initially transcripted at TO (end of Logarithmic growth phase) and keeping expression in stationary phase. Beta-galactosidase assay of cry1Ac'-lacZ and SDS-PAGE indicated that expression of cry1Ac gene in HD73 (delta nprR) was stronger than that in HD-73 during transition phase and early stationary phase. However, Cry expressed product between HD-73 and HD73 (delta nprR) in LB medium has no significant difference when crystal and spore were released.

Conclusion: The deletion of nprR increased expression and transcription activity of cry1Ac during transition and early stationary phase in rich media.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus thuringiensis / genetics
  • Bacillus thuringiensis / growth & development
  • Bacillus thuringiensis / physiology*
  • Bacillus thuringiensis Toxins
  • Bacterial Proteins / genetics*
  • Bacterial Proteins / metabolism
  • Endotoxins / genetics*
  • Endotoxins / metabolism
  • Gene Deletion*
  • Gene Expression Regulation, Bacterial*
  • Genes, Regulator*
  • Hemolysin Proteins / genetics*
  • Hemolysin Proteins / metabolism
  • Quorum Sensing*

Substances

  • Bacillus thuringiensis Toxins
  • Bacterial Proteins
  • Endotoxins
  • Hemolysin Proteins
  • insecticidal crystal protein, Bacillus Thuringiensis