Two bacteriophages which utilize a new Escherichia coli major outer membrane protein as part of their receptor.

Chai, Tuu-Jyi; Foulds, John

doi:10.1128/jb.135.1.164-170.1978

Cited by 78 publications

(30 citation statements)

References 25 publications

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“…Similarly, all the mutant proteins were protected when cell envelopes were treated with trypsin (Figure 1A), indicating that they were correctly assembled. Furthermore, wild‐type PhoE functions in the outer membrane as the receptor for phage TC45 (Chai and Foulds, 1978). CE1265 cells expressing either one of the mutant PhoE proteins were sensitive to this phage (data not shown), which confirms that the mutant proteins were correctly assembled.…”

Section: Resultsmentioning

confidence: 99%

Folding of a bacterial outer membrane protein during passage through the periplasm

Eppens

1997

The EMBO Journal

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The transport of bacterial outer membrane proteins to their destination might be either a one‐step process via the contact zones between the inner and outer membrane or a two‐step process, implicating a periplasmic intermediate that inserts into the membrane. Furthermore, folding might precede insertion or vice versa. To address these questions, we have made use of the known 3D‐structure of the trimeric porin PhoE of Escherichia coli to engineer intramolecular disulfide bridges into this protein at positions that are not exposed to the periplasm once the protein is correctly assembled. The mutations did not interfere with the biogenesis of the protein, and disulfide bond formation appeared to be dependent on the periplasmic enzyme DsbA, which catalyzes disulfide bond formation in the periplasm. This proves that the protein passes through the periplasm on its way to the outer membrane. Furthermore, since the disulfide bonds create elements of tertiary structure within the mutant proteins, it appears that these proteins are at least partially folded before they insert into the outer membrane.

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Section: Resultsmentioning

confidence: 99%

Folding of a bacterial outer membrane protein during passage through the periplasm

Eppens

1997

The EMBO Journal

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“…coli HJM114 (dlac pro) F' (lac pro), UT580 ri mi TnlO dlac proAB, supD, F' (traD36 lac(IqZM15 proAB), and JM103 (dlac pro, thi, strA, supE, endA, sbcB) F'(traD36, lacPM15 proAB) were from our collection. JF699 (proC24,ompA252,his53,purE41,ilv277,met65,lacY29,xy114,rpsL97 cycAl,cycB2,tsx63, has been described (Chai and Foulds, 1978). Plasmid pQN120 encoding the AraB -pro-OmpA fusion protein was constructed as follows.…”

Section: Materials and Methods Bacterial Strains And Plasmidsmentioning

confidence: 99%

“…4). In this study we measured the kinetics of processing in the E. coli strain JF699 which has a defective chromosomal copy of the OmpA gene (Chai and Foulds, 1978). Fig.…”

Section: Positional Dependency Of Positively Charged Residues On Protmentioning

confidence: 99%

Evidence for a Loop‐Like Insertion Mechanism of Pro‐Omp A into the Inner Membrane of Escherichia Coli

Kühn¹,

Kiefer²,

Köhne³

et al. 1994

European Journal of Biochemistry

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We have studied the insertion of pro-OmpA into the Escherichia coli membrane in vivo using various mutants that have either alterations in the amino-terminal parts of the signal peptide or in the mature region that flanks the signal peptide. A pro-OmpA mutant with an amino terminal extension of 142 residues derived from ribulokinase (AraB) was analysed for its membrane insertion. The AraB portion, which includes a cluster of seven charged residues close to the signal sequence, did not interfere with the Sec components and allowed efficient export of OmpA. During translocation the AraB portion remained in the cytoplasm. Further mutants of OmpA were constructed in the carboxy-terminal region flanking the signal sequence. Pro-OmpA does not translocate across the membrane when a charge cluster, comprised of Lys-Arg-Arg-Glu-Arg, is introduced after positions 5, 11 or 15 of the mature region, but is translocated when the cluster is introduced after position 22. This defines a region of about 20 residues in the mature part of pro-OmpA that is crucial for membrane insertion. These results suggest that in the case of the Sec-dependent proOmpA, as with the Sec-independent M13 procoat, the precursor assumes a loop-like structure involving the signal peptide and the early part of the mature region, leaving the amino terminus of the signal peptide at the cytoplasmic face.

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“…Incubation was continued at 30 or 37°C overnight. Bacteriophage sensitivity and absorption were tested as described elsewhere (9). Transport assays.…”

Section: Methodsmentioning

confidence: 99%

Co-Regulation in Escherichia coli of a Novel Transport System for sn -Glycerol-3-Phosphate and Outer Membrane Protein Ic (e, E) with Alkaline Phosphatase and Phosphate-Binding Protein

Argast

Boos

1980

J Bacteriol

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Mutants constitutive for the novel outer membrane protein Ic (e or E) contained a recently discovered binding protein for sn-glycerol-3-phosphate. The corresponding parental strains missing the outer membrane protein Ic (e, E) were negative or strongly reduced in the synthesis of the binding protein. In addition, strains that were previously isolated as mutants constitutive for the sn-glycerol-3-phosphate transport system (ugp+ mutants) and that produced the novel periplasmic proteins GP1 to GP4 also synthesized a new outer membrane protein with the same electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gels as protein Ic. Screening of different ugp+ mutants revealed the existence of three types in respect to the four novel periplasmic proteins GP1, -2, -3, and -4: (i) one containing all four proteins; (ii) one containing only proteins GP1, -2, and -3; (iii) one containing only proteins GP1, -2, and -4. In confirmation of the data presented in the accompanying paper by Tommassen and Lugtenberg (J. Bacteriol. 143:151-157, 1980), we found that purified GP1 is identical to alkaline phosphatase, whereas purified GP3 has binding activity of inorganic phosphate and is identical to the phosphate-binding protein. Moreover, growth conditions that lead in a wild-type strain to the derepression of alkaline phosphatase synthesis also derepressed the synthesis of the sn-glycerol-3-phosphate-binding protein as well as the corresponding transport system. Thus, the new sn-glycerol-3-phosphate transport system is part of the alkaline phosphatase regulatory system.Recently, we found a new transport system for sn-glycerol-3-phosphate (G3P) in mutants (ugp+ mutants) that arose as G3P+ suppressors in strains carrying a defective transport system for G3P coded for by gipT (3) at 48 min on the Escherichia coli chromosome (4). These ugp+ mutants mapped outside gipT and synthesized the new periplasmic proteins (GP1, -2, and -3). One of these proteins (GP2) was identified as a high-affinity binding protein for G3P (2).Along other lines, we were interested in the pore-forning activity of osmotic shock fluid in black lipid films due to soluble outer membrane proteins Ia and lb (6). In this respect, we were interested whether or not the newly discovered outer membrane protein Ic (18) also exhibited pore-forming activity when shock fluids of this mutant were used in the black lipid pore assay. Although this was indeed the case (R. Benz and U. Henning, manuscript in preparation) we noticed that the periplasmic proteins of the Iccarrying strain exhibited a polyacrylamide gel pattern very similar to those obtained from shock fluids of our G3P+ ugp+ mutants. 142

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Two bacteriophages which utilize a new Escherichia coli major outer membrane protein as part of their receptor.

Cited by 78 publications

References 25 publications

Folding of a bacterial outer membrane protein during passage through the periplasm

Folding of a bacterial outer membrane protein during passage through the periplasm

Evidence for a Loop‐Like Insertion Mechanism of Pro‐Omp A into the Inner Membrane of Escherichia Coli

Co-Regulation in Escherichia coli of a Novel Transport System for sn -Glycerol-3-Phosphate and Outer Membrane Protein Ic (e, E) with Alkaline Phosphatase and Phosphate-Binding Protein

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