Insertional inactivation of the Staphylococcus aureus beta-toxin by bacteriophage phi 13 occurs by site- and orientation-specific integration of the phi 13 genome

Mol Microbiol. 1991 Apr;5(4):933-9. doi: 10.1111/j.1365-2958.1991.tb00768.x.

Abstract

Lysogenization of Staphylococcus aureus by the serotype F converting bacteriophage phi 13 results in loss of beta-toxin expression. Sequence analysis of the S. aureus beta-toxin gene (hlb), the attachment site (attP)-containing region of phi 13 DNA and the chromosome/bacteriophage DNA junctions of a phi 13 lysogen, revealed that the molecular mechanism of loss of beta-toxin expression was due to insertion of the phi 13 genome into the 5' end of hlb. The insertion site (attB) within hlb contained a 14 base pair core sequence in common with attP and both ends of the integrated linear prophage genome of a phi 13 lysogen. These findings indicate that integration of the phi 13 genome into hlb is site- and orientation-specific.

MeSH terms

  • Amino Acid Sequence
  • Attachment Sites, Microbiological
  • Bacterial Toxins / genetics*
  • Base Sequence
  • Chromosomes, Bacterial
  • Hemolysin Proteins
  • Lysogeny*
  • Molecular Sequence Data
  • Mutagenesis, Insertional
  • Polymerase Chain Reaction
  • Restriction Mapping
  • Sphingomyelin Phosphodiesterase*
  • Staphylococcus Phages / genetics*
  • Staphylococcus aureus / genetics*

Substances

  • Bacterial Toxins
  • Hemolysin Proteins
  • Sphingomyelin Phosphodiesterase
  • hlb protein, Staphylococcus aureus