Mutants of <i>Escherichia coli</i> K12 lacking all ‘major’ proteins of the outer cell envelope membrane

Henning, Ulf; Haller, I.

doi:10.1016/0014-5793(75)80983-5

Cited by 116 publications

(65 citation statements)

References 21 publications

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“…1. The results of scanning of the gels (Table II) show that the amount of pore protein expressed either relative to OmpA protein or to total cell envelope protein is practically constant whereas the amount of OmpA protein over the amount of total cell envelope protein is 2-fold higher in the pore protein deficient strain than in the other three strains, consistent with data reported earlier [35][36][37][38][39] [12]. b + and -, present and absent, respectively, during the uptake experiment after growth under the described conditions.…”

Section: Phn Isupporting

confidence: 90%

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 Isupporting

confidence: 90%

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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“…The vector used in the initial cloning was iNM590 [14], subcloning was accomplished using the low-copy number vector, pHSG415 [15] [7,8,16]. Crude preparations of colicin L-JF246, K-K235 and bacteriocin 4-59 were produced by the method of Foulds [17].…”

Section: Bacteria Phages Plasmids and Colicinsmentioning

confidence: 99%

“…In Escherichia coli this transmembrane protein mediates in F-dependent conjugation [2 -41 and confers stability on the outer membrane [5]. It has also been adopted as the cell surface receptor by a group of T-even-like bacteriophages, including K3, TuII* and 0x2 [6,7] and is required for the uptake of certain colicins [8]. In a recent study [9] with two mutant derivatives of the cloned ompA gene a region of the protein was identified which is essential for the binding of phages K3 and TuII* to occur.…”

mentioning

confidence: 99%

Cloning and Molecular Characterization of the ompA Gene from Salmonella typhimurium

Freudl

Cole

1983

European Journal of Biochemistry

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The ompA gene from Salmonella typhimurium, encoding a major heat‐modifiable protein of the outer membrane, has been cloned and extensively characterized. When expressed in Escherichia coli the gene directs the synthesis of an OmpA protein which is functionally and topologically indistinguishable from that made in S. typhimurium, thus indicating that export and membrane incorporation are very similar in the two organisms. The S. typhimurium protein effectively substitutes for the E. coli polypeptide in F‐dependent conjugation and in the uptake of certain colicins, although it cannot serve as the receptor for the OmpA‐specific phages K3 and Tull*. On examination of the primary sequence of the protein, predicted from the nucleotide sequence of its gene, it was found that those domains likely to be exposed on the cell surface were significantly different to the corresponding regions of the E. coli polypeptide. These differences in the structure of the two proteins have been used to interpret differences in their biological activities.

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“…Aside from several minor bands, lipoprotein, large amounts of protein II*, probably some protein I, and another protein in the 70 000-80 000 dalton range were recovered. That the protein designated in f&lb in fact represents this protein could easily be verified by using a mutant in the aroD background missing the protein (obtained by selection for resistance to phage TuII*, [ 181): no protein of this electrophoretic position could be linked to the murein of the mutant.…”

Section: Crosslinking Of Protein Ii* To the Murein Layermentioning

confidence: 99%

Major outer membrane proteins of Escherichia coli K‐12: Evidence for Protein II* being a transmembrane protein

1978

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Mutants of Escherichia coli K12 lacking all ‘major’ proteins of the outer cell envelope membrane

Cited by 116 publications

References 21 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

Cloning and Molecular Characterization of the ompA Gene from Salmonella typhimurium

Major outer membrane proteins of Escherichia coli K‐12: Evidence for Protein II* being a transmembrane protein

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