Keywords:
Porin
Wild-type Escherichia coli K-12 produces two porins, OmpF (protein 1a) and OmpC (protein 1b). In mutants deficient in both of these "normal" porins, secondary mutants that produce a "new" porin, protein PhoE (protein E), are selected for. We determined the properties of the channels produced by each of these porins by measuring the rates of diffusion of various cephalosporins through the outer membrane in strains producing only one porin species. We found that all porin channels retarded the diffusion of more hydrophobic cephalosporins and that with monoanionic cephalosporins a 10-fold increase in the octanol-water partition coefficient of the solute produced a 5- to 6-fold decrease in the rate of penetration. Electrical charges of the solutes had different effects on different channels. Thus, with the normal porins (i.e., OmpF and OmpC proteins) additional negative charge drastically reduced the penetration rate through the channels, whereas additional positive charge significantly accelerated the penetration. In contrast, diffusion through the PhoE channel was unaffected by the presence of an additional negative charge. We hypothesize that the relative exclusion of hydrophobic and negatively charged solutes by normal porin channels is of ecological advantage to E. coli, which must exclude hydrophobic and anionic bile salts in its natural habitat. The properties of the PhoE porin are also consistent with the recent finding (M. Argast and W. Boos, J. Bacteriol. 143:142-150, 1980; J. Tommassen and B. Lugtenberg, J. Bacteriol. 143:151-157, 1980) that its biosynthesis is derepressed by phosphate starvation; the channel may thus act as an emergency pore primarily for the uptake of phosphate and phosphorylated compounds.
Porin
Colicin
Penetration (warfare)
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Citations (371)
The relative amounts of the OmpF and OmpC proteins in the outer membrane of Escherichia coli K-12 are affected differentially by high concentrations of substances like sucrose in culture media in such a manner that a decrease in the amount of the OmpF protein appears to be compensated for by a reciprocal increase in the OmpC protein. When an ompF mutation was introduced, OmpC synthesis became almost independent of sucrose and occurred at the fully induced level even in the absence of sucrose. On the other hand, introduction of an ompC mutation did not affect the sucrose-dependent profile of OmpF synthesis. The effect of the ompF mutation was also examined with the ompC-lac fusion strain, in which expression of beta-galactosidase is under the control of the ompC promoter. The expression of beta-galactosidase coded for by the ompC-lac fusion in the ompF+ and ompF- strains was essentially the same as that of the OmpC protein, being sucrose dependent in the ompF+ strain and sucrose-independent in the ompF mutant. From these results we conclude that sucrose in the medium primarily regulates ompF gene expression, which in turn regulates ompC gene expression at the transcriptional level. This sequential regulatory mechanism is discussed in relation to the function of the ompB locus.
Porin
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Citations (35)
Escherichia coli K-12 produces both the OmpF and OmpC porins, the relative amounts of which in the outer membrane are affected in a reciprocal manner by the osmolarity of the growth medium. In contrast, E. coli B produces only the OmpF porin, regardless of the medium osmolarity. In this study, it was revealed that there is an extensive deletion within the ompC locus of the E. coli B chromosome. Cloning and nucleotide sequencing of the regulatory gene, ompR, of E. coli B revealed that there are two amino acid alterations (Lys-6 to Asn and Ala-130 to Thr) in the amino acid sequence of the OmpR protein, as compared with that of E. coli K-12. It is suggested that these particular amino acid alterations are responsible for the constitutive expression of the ompF gene observed in E. coli B.
Porin
Osmotic concentration
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The OmpC, OmpF, and Lc (NmpC) porin proteins of Escherichia coli K-12 have been shown to be similar to the OmpC (36K), OmpF (35K) and OmpD (34K) porin proteins of Salmnella typhimurium LT2 in terms of function, regulation of expression, and, in the case of OmpC and OmpF proteins, equivalence of the genetic loci determining their production. However, the corresponding pairs of proteins from these two species showed only limited similarity in peptide maps and no similarity in terms of migration on polyacrylamide gels.
Porin
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Citations (35)
The roles of OmpC and OmpF in acidic resistance (AR) were examined. When ompC and ompF were deleted, AR was decreased. The decreased level of AR seen in the mutant that was deficient in ompC and ompF was elevated by the addition of glutamate, but not by the addition of arginine or lysine. The expression levels of adiA and cadB were diminished by the deletion of ompC and ompF, and the conversion of arginine to agmatine and lysine to cadaverine by intact cells were reduced in the mutant. The expression of gadA/gadB was not affected by the deletion of ompC and ompF. These results suggest that the transport of arginine, lysine, and their decarboxylated products through OmpC and/or OmpF is essential for the survival of Escherichia coli cells under extremely acidic conditions.
Lysine decarboxylase
Agmatine
Arginine decarboxylase
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Citations (35)
Porin
Strain (injury)
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The outer membrane (OM) vitamin B 12 receptor, BtuB, is the primary receptor for E group colicin adsorption to Escherichia coli . Cell death by this family of toxins requires the OM porin OmpF but its role remains elusive. We show that OmpF enhances the ability of purified BtuB to protect bacteria against the endonuclease colicin E9, demonstrating either that the two OM proteins form the functional receptor or that OmpF is recruited for subsequent translocation of the bacteriocin. While stable binary colicin E9–BtuB complexes could be readily shown in vitro, OmpF‐containing complexes could not be detected, implying that OmpF association with the BtuB–colicin complex, while necessary, must be weak and/or transient in nature.
Colicin
Porin
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Citations (17)
Various ompF-ompC, ompC-ompF, and ompF-ompC-ompF chimeric genes were used to locate the domains of the OmpF protein involved in cellular sensitivity to colicins. Various parts of the porin participate in the entry of colicins. Colicin N receptor activity was found to require three regions: RN1, located between residues 1 and 63; RN2, located between residues 115 and 262; and RN3, located between residues 279 and 297. The central domain from residues 143 to 262 is involved during the translocation step after the binding step. A large region, including residues 1 to 262, is necessary during colicin A entry. The locations and interactions between these domains specifically required for the uptake of colicins to occur are described and discussed with regard to the homology and topology of the OmpC, OmpF, and PhoE porins.
Colicin
Porin
Homology
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Citations (42)
The effects of growth conditions on the expression of the Escherichia coli K-12 major outer membrane porin gene ompF were determined by measuring the amount of OmpF protein incorporated into the outer membrane, β-galactosidase activity in cells in which lacZ was regulated by the ompF promoter, and by studying their effects in the presence of the general transcription inhibitor rifampicin. A variety of conditions reduced ompF transcription. Common features among the inhibitors of ompF expression could not be identified; another protease inhibitor and another uncoupler did not specifically affect ompF expression. It is therefore concluded that the inhibitors interact directly or indirectly with a sensory system (possibly EnvZ protein) which affects the porin gene regulon accordingly.
Porin
Regulon
Transcription
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Carbenicillin-resistant mutants of Escherichia coli K-12 and B/r were found to produce greatly diminished levels of the porin coded by the ompF gene. Physiological and ecological implications of these findings are discussed.
Porin
Carbenicillin
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Citations (178)