Role of the Arg158 residue of the outer membrane PhoE pore protein of Escherichia coli K 12 in bacteriophage TC45 recognition and in channel characteristics

Eur J Biochem. 1985 Nov 4;152(3):691-7. doi: 10.1111/j.1432-1033.1985.tb09249.x.


In order to study the structure-function relationship of the PhoE protein pore we have isolated five independent, TC45-resistant, phoE mutants all of which appeared to produce normal amounts of an electrophoretically altered PhoE protein, designated as PhoE* protein. Nucleotide sequence analysis of the DNA fragments carrying the mutations showed that the mutations all correspond to a G.C to A.T transition at the same place within the phoE gene resulting in a deduced change of amino acid residue arginine 158 into histidine. This result shows that the arginine 158 residue plays an important role in the interaction of the PhoE protein pore with phage TC45. Moreover, studies on the channel properties of the PhoE* protein showed that the PhoE channel has lost part of its preference for negatively charged solutes, as a result of the arginine to histidine change. The results are discussed in terms of the structure-function relationship of PhoE protein as well as in terms of the topological organization of the protein channel in the outer membrane.

MeSH terms

  • Arginine / physiology*
  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / physiology*
  • Base Sequence
  • Coliphages / physiology*
  • DNA, Bacterial / isolation & purification
  • Electrochemistry
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / genetics
  • Escherichia coli / physiology*
  • Genes
  • Ion Channels / physiology
  • Mutation


  • Bacterial Outer Membrane Proteins
  • DNA, Bacterial
  • Ion Channels
  • Arginine