The ompR transcription is induced directly by its own gene product in Salmonella enterica [3]. OmpR consensus-like sequences are found in the upstream region of ompR in Escherichia coli, although there are still no reported experimental data for its FG-4592 manufacturer autoregulation in this bacterium. Upon the elevation of medium osmolarity, cellular OmpR-P levels are likely enhanced by two distinct mechanisms, namely, post-translational phosphorylation/dephosphorylation by EnvZ and transcriptional auto-stimulation. Enterobacteriaceae express at least two major outer membrane (OM) porins, namely,

OmpF and OmpC, both of which form transmembrane pore structures and function as ion channel [4–6]. OmpF and OmpC in the cell of E. coli form water-filled pores that are poorly selective EPZ004777 molecular weight to cations (so called non-specific porins), thereby allowing the diffusion of low-molecular-weight polar compounds (not over 600 daltons) into the cell to maintain cell permeability. They exist as homotrimers in the OM. The basic structural element of the porin monomer is an ellipsoid in the section cylinder consisting of 16 transmembrane β-strands (so-called β-barrel)

connected by short periplasmic and longer ‘external’ www.selleckchem.com/products/crt0066101.html loops [7]. E. coli OmpX contains 8-stranded β-barrel, with polar residues on the inside and hydrophobic residues on the outside facing the membrane environment [8]. Enterobacter aerogenes OmpX is the smallest known channel protein with a markedly cationic selectivity [6, 9, 10]. Although several experiments have demonstrated that OmpX plays Molecular motor roles that are similar to those of porin [6, 9–12], it is not yet clear whether or not OmpX forms porins on the

cell membrane. E. aerogenes OmpX forms channels in the lipid bilayer [6]; however, the NMR and crystal structures of OmpX do not show pores [8, 13]. The ompX expression in E. coli [12] or E. aerogenes [6] is enhanced during early exposure to environmental perturbations, such as high osmolarity, antibiotics and toxic compounds, that are accompanied by the repressed expression of non-specific porins (OmpF and/or OmpC). Over-expression of OmpX, with a channel structure that is much smaller than that of OmpF and OmpC [6], may stabilize cell OM and balance the decreased expression of the two non-specific porins for the exclusion of small harmful molecules. It is interesting to further investigate the roles of OmpX in modulating OM permeability and adaptability. OmpR consensus-like sequences have been found within the ompX upstream region in E. coli and E. aerogenes [6]; however, the regulation of ompX by OmpR has not yet been established experimentally in any bacterium. As shown in E. coli as a model, OmpF and OmpC are reciprocally regulated by medium osmolarity.