Butyricin 7423 and the membrane H+ -ATPase of Clostridium pasteurianum

Arch Microbiol. 1982 Feb;131(1):81-6. doi: 10.1007/BF00451503.


The bacteriocin butyricin 7423 inhibited the activity of the membrane H+ -ATPase (BFoF1) of vegetative cells of Clostridium pasteurianum but not that of its soluble BF1 component. In vitro studies with the H+-ATPases of mutant strains selected for diminished sensitivity sensitivity (a) to butyricin 7423 and (b) to dicyclohexylcarbodi-imide, confirmed that butyricin 7423 interacts with the BFo component of this enzyme complex. Even so, certain other mutant strains displaying decreased sensitivity to butyricin 7423 possessed H+-ATPases which in vitro showed undiminished sensitivity to inhibition by the bacteriocin. Furthermore, from the changes in intracellular ATP concentration and in the rates and net extent of efflux of intracellular 86Rb+ ions that were provoked by exposure of the parent and several of the mutant strains to butyricin 7423, it was concluded that its primary bactericidal action was not attributable to stoichiometric inhibition of the membrane H+-ATPase. High extracellular concentrations of K+ ions enabled Cl. pasteurianum to survive exposure to low concentration of this membrane active bacteriocin.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Adenosine Triphosphate / metabolism
  • Bacterial Proteins / pharmacology*
  • Bacteriocins / pharmacology*
  • Clostridium / drug effects*
  • Clostridium / enzymology
  • Clostridium / metabolism
  • Dicyclohexylcarbodiimide / pharmacology
  • Mutation
  • Potassium / metabolism
  • Rubidium / metabolism


  • Bacterial Proteins
  • Bacteriocins
  • Dicyclohexylcarbodiimide
  • butyricin 7423
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • Rubidium
  • Potassium