Two HlyIIR dimers bind to a long perfect inverted repeat in the operator of the hemolysin II gene from Bacillus cereus

FEBS Lett. 2007 Mar 20;581(6):1190-6. doi: 10.1016/j.febslet.2007.02.035. Epub 2007 Feb 28.


HlyIIR is a negative transcriptional regulator of hemolysin II gene from B. cereus. It binds to a long DNA perfect inverted repeat (44bp) located upstream the hlyII gene. Here we show that HlyIIR is dimeric in solution and in bacterial cells. No protein-protein interactions between dimers and no significant modification of target DNA conformation upon complex formation were observed. Two HlyIIR dimers were found to bind to native operator independently with Kd level in the nanomolar range. The minimal HlyIIR binding site was identified as a half of the long DNA perfect inverted repeat.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacillus cereus / genetics*
  • Bacterial Proteins / genetics*
  • Bacterial Toxins / genetics*
  • Binding Sites
  • Dimerization
  • Genes, Bacterial
  • Hemolysin Proteins / genetics*
  • Nucleic Acid Conformation
  • Operator Regions, Genetic*
  • Protein Binding
  • Repetitive Sequences, Nucleic Acid*


  • ApxII toxin, bacteria
  • Bacterial Proteins
  • Bacterial Toxins
  • Hemolysin Proteins