Genetic identification of the pore domain of the OmpC porin of Escherichia coli K-12

@article{Misra1988GeneticIO,
  title={Genetic identification of the pore domain of the OmpC porin of Escherichia coli K-12},
  author={Rajeev Misra and Spencer A. Benson},
  journal={Journal of Bacteriology},
  year={1988},
  volume={170},
  pages={3611 - 3617}
}
We have isolated and characterized 31 mutations in the ompC gene which allow Escherichia coli to grow on maltotriose (Dex+) in the absence of the LamB and OmpF porins. These ompC(Dex) mutations include single-base-pair substitutions, small deletions, and small insertions. DNA sequence analysis shows that all of the alterations occur within the coding region for the first 110 amino acids of mature OmpC. The 26 independent point mutations repeatedly and exclusively alter residues R37, R74, and… 
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Mutations that alter the pore function of the OmpF porin of Escherichia coli K12.
A novel mutation, cog, which results in production of a new porin protein (OmpG) of Escherichia coli K-12
TLDR
It is proposed that the cog mutation destroys a negative regulatory function and therefore derepresses ompG expression and is a porinlike protein.
OmpF assembly mutants of Escherichia coli K-12: isolation, characterization, and suppressor analysis
  • R. Misra
  • Biology
    Journal of bacteriology
  • 1993
TLDR
The results presented in this study raise the intriguing possibility of a chaperone-like activity for the wild-type suppressor gene product of OmpF.
Isolation and preliminary characterization of wild-type OmpC porin dimers from Escherichia coli K-12.
TLDR
Electrical conductance across planar bilayer lipid membranes and liposome swelling assays showed that the two isolates had similar channel-forming activity, and circular dichroism spectra of isolated dimers and trimers indicated similar amounts of beta-structure.
Identification and characterization of a new gene of Escherichia coli K-12 involved in outer membrane permeability.
TLDR
A general cloning strategy that can be used to clone both dominant and recessive alleles and alter the permeability of the outer membrane resulting in increased sensitivity to detergents, antibiotics and dyes is described.
Structural and functional characterization of the OmpF and OmpC porins of the Escherichia coli outer membrane: studies involving chimeric proteins.
Phenotypic Characterization of Pore Mutants of the Vibrio cholerae Porin OmpU
TLDR
The results indicate that specific residues play different roles in controlling the passage of various compounds, including sensitivity to beta-lactam antibiotics, growth on large sugars, and biofilm induction by sodium deoxycholate.
Biochemistry and Regulation of a NovelEscherichia coli K-12 Porin Protein, OmpG, Which Produces Unusually Large Channels
TLDR
The folding model of OmpG suggests that it is the first 16-stranded beta-barrel porin that lacks the large external loop, L3, which constricts the channels of other nonspecific and specific porins.
Assembly-defective OmpC mutants of Escherichia coli K-12
TLDR
One novel OmpC mutant was investigated in which an assembly defect was caused by a disulfide bond formation between two nonnative cysteine residues, and this defect was fully corrected in a genetic background in which the cell's ability to form disulfides bonds was compromised.
Characterization of ompF domains involved in Escherichia coli K-12 sensitivity to colicins A and N
TLDR
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.
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References

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TLDR
The results suggest that this region of the OmpC protein is involved in the pore domain and that the alterations lead to an increased pore size.
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TLDR
A series of ompC‐phoE hybrid genes in which the DNA encoding part of one protein is replaced by the corresponding part of the other gene are constructed to study the structure‐function relationship of these proteins.
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
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