PhoE protein pores in the outer membrane of Escherichia coli K-12 not only have a preference for Pi and Pi-containing solutes but are general anion-preferring channels

Abstract

Previous studies on the question of whether the PhoE protein pore has a preference for Pi and Pi-containing solutes only or whether it constitutes a general anion-preferring channel, have not given an unequivocal answer either because the presence of the phosphate binding protein was not ascertained or because only arsenate was tested as a non Pi-containing control solute. Permeability properties of PhoE, OmpF and OmpC protein pores for negatively charged solutes were measured in vivo in the presence of phosphate-binding protein. It appeared that the PhoE protein pore is the most efficient channel for the three tested solutes phosphate, succinate and sulphate. Conditions were established to measure the frequency of ethyl methane sulphonate induced mutations as a function of the presence of pore proteins. These results indicate that PhoE protein also forms the most efficient channel for ethyl methane sulphonate. We conclude that the preference of the PhoE protein pore is not restricted to Pi and Pi-containing solutes but also concerns several other negatively charged solutes.