Pore protein e of the outer membrane of <i>escherichia coli</i> K12

Lugtenberg, Ben; Boxtel, Ria van; Verhoef, Cornelis; Alphen, Wim Van

doi:10.1016/0014-5793(78)81071-0

Cited by 42 publications

(35 citation statements)

References 37 publications

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“…Only the relevant part of the gel is shown. Protein a is a minor outer membrane protein with approximately the same electrophoretic mobility as PhoE protein [10]. LamB protein functions as a pore with substrate specificity for maltose and maltodextrins [32].…”

Section: Phn Imentioning

confidence: 99%

“…This explains why the rate of permeation through the outer membrane is the limiting step in an uptake assay only at very low solute concentrations, usually in the gM range [3,4,6,10,40]. Fig.…”

Section: In Vivo Rates Of Pi Permeation Through Phoe Protein Poresmentioning

confidence: 99%

“…Growth of E. coli under conditions of phosphate limitation results in derepression of the synthesis of a new outer membrane protein [8] which is antigenically related to the other two pore proteins [1]. This protein has previously been designated as protein Ic [9], e [10] or E [11] but should be named PhoE protein [12] as according to the new uniform nomenclature system these proteins are designated after their structural gene [ 13]. In addition to PhoE protein, the cell synthesizes a large number of other proteins [14,15] as a reaction on phosphate limitation, e.g.…”

Section: Introductionmentioning

confidence: 99%

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PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

Korteland

Tommassen

Lugtenberg

1982

Biochimica et Biophysica Acta (BBA) - Biomembranes

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This study was undertaken to investigate the proposed in vivo pore function of PhoE protein, an Escherichia coil KI2 outer membrane protein induced by growth under phosphate limitation, and to compare it with those of the constitutive pore proteins OmpF and OmpC. Appropriate mutant strains were constructed containing only one of the proteins PhoE, OmpF or OmpC, or none of these proteins at all. By measuring rates of nutrient uptake at low solute concentrations, the proposed pore function of PhoE protein was confirmed as the presence of the protein facilitates the diffusion of Pi through the outer membrane, such that a pore protein deficient strain behaves as a K m mutant. Comparison of the rates of permeation of Pi, glycerol 3-phosphate and glucose 6-phosphate through pores formed by PhoE, OmpF and OmpC proteins shows that PhoE protein is the most effective pore in facilitating the diffusion of Pi and phosphorus-containing compounds. The three types of pores were about equally effective in facilitating the permeation of glucose and arsenate. Possible reasons for the preference for Pi and Pi-containing solutes are discussed.

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Section: Phn Imentioning

confidence: 99%

Section: In Vivo Rates Of Pi Permeation Through Phoe Protein Poresmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

Korteland

Tommassen

Lugtenberg

1982

Biochimica et Biophysica Acta (BBA) - Biomembranes

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“…It can be isolated associated with the peptidoglycan layer [8,13] and it is immunologically related to OmpF and OmpC protein [14], the latter being consistent with the recently observed strong homology in primary structure between OmpC protein, OmpF protein and PhoE protein [15,16]. PhoE protein functions as a general pore like OmpF and OmpC protein [6,8,13,17,18]. Besides general pore properties, PhoE protein has a preference for Pi and Pi-containing solutes as was shown by in vivo transport assays carried out at low solute concentration [19].…”

Section: Introductionmentioning

confidence: 99%

“…In mutants devoid of lipoprotein severe physiological and morphological alterations occur [22]. Mutants with heptoseless lipopolysaccharide have largely diminished amounts of OmpF protein [23][24][25][26] and PhoE protein [13]. Data of Schindler et al [27] show that interaction between lipopolysaccharide and OmpF protein is essential for the functioning of this pore protein.…”

Section: Introductionmentioning

confidence: 99%

Increased efficiency of the outer membrane PhoE protein pore in escherichia coli K-12 mutants with heptose-deficient lipopolysaccharide

Korteland

Lugtenberg

1984

Biochimica et Biophysica Acta (BBA) - Biomembranes

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The pore properties of PhoE protein channels in the outer membrane of a lipoprotein-deficient mutant and in a mutant with heptose-deficient lipopolysaecharide were investigated. The absence of lipoprotein neither affects the rate of permeation of glucose 6-phosphate or of the/~-lactam antibiotic eephsulodin through the PhoE pore nor the inhibition of cephsulodin permeation by polyphosphate. In contrast, heptose deficiency results in a 6-to 8-fold increase in the rates of permeation of glucose 6-phosphate and cephsulodin. Possible explanations for these data are discussed. It is argued that the lipopolysaecharide structure synthesized under phosphate limitation may be similar to that of the heptoseless mutant and hence that not only the structure of the PhoE protein pore but also the structure of the lipopolysaecharide may promote the uptake of Pi and Pi-containing solutes under phosphate limitation.

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The ultimate localization of an outer membrane protein of Escherichia coli K-12 is not determined by the signal sequence.

1983

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To study the role of the signal sequences in the biogenesis of outer membrane proteins, we have constructed two hybrid genes: a phoE‐ompF hybrid gene, which encodes the signal sequence of outer membrane PhoE protein and the structural sequence of outer membrane OmpF protein, and a bla‐phoE hybrid gene which encodes the signal sequence as well as 158 amino acids of the structural sequence of the periplasmic enzyme beta‐lactamase and the complete structural sequence of PhoE protein. The products of these genes are normally transported to and assembled into the outer membrane These results show: (i) that signal sequences of exported proteins are export signals which function independently of the structural sequence, and (ii) that the information which determines the ultimate location of an outer membrane protein is located in the structural sequence of this protein, and not in the signal sequence.

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Pore protein e of the outer membrane of escherichia coli K12

Cited by 42 publications

References 37 publications

PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

PhoE protein pore of the outer membrane of Escherichia coli K12 is a particularly efficient channel for organic and inorganic phosphate

Increased efficiency of the outer membrane PhoE protein pore in escherichia coli K-12 mutants with heptose-deficient lipopolysaccharide

The ultimate localization of an outer membrane protein of Escherichia coli K-12 is not determined by the signal sequence.

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