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Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure.
It seems that cleavage of only one peptide bond adjacent to the lysine link between the lipoprotein and the murein causes the rapid decrease of the absorbance and as shown by electron microscopic exmination of ultrathin sections of trypsin treated cell walls, two separated membrane structures appear which otherwise are closely adjacent to one another.
Bacterial iron transport: mechanisms, genetics, and regulation.
Bacterial solutions to the iron-supply problem.
Surface Signaling in Ferric Citrate Transport Gene Induction: Interaction of the FecA, FecR, and FecI Regulatory Proteins
In Escherichia coli, transcription of the ferric citrate transport genes fecABCDE is controlled by a novel signal transduction mechanism that starts at the cell surface and interaction of the cytoplasmic N terminus of FecR with FECI, which results in FecI activation.
The structurally related exbB and tolQ genes are interchangeable in conferring tonB-dependent colicin, bacteriophage, and albomycin sensitivity
- V. Braun
- BiologyJournal of bacteriology
- 1 November 1989
Cells carrying mutations in exbB were partially tolerant to colicins B, D, and M and became fully tolerant by the introduction of tolQ mutations, which suggested involvement of bothExbB and tol Q in tonB-dependent uptake.
Covalent lipoprotein from the outer membrane of Escherichia coli.
- V. Braun
- BiologyBiochimica et biophysica acta
- 31 October 1975
Iron uptake mechanisms and their regulation in pathogenic bacteria.
- V. Braun
- EconomicsInternational journal of medical microbiology…
The few principal mechanisms that underly the large variety of iron supply systems will be presented, as well as cases, in which definedIron supply systems are related to virulence.
Ton-dependent colicins and microcins: modular design and evolution.
Regulation of citrate‐dependent iron transport of Escherichia coli: FecR is required for transcription activation by Feel
- M. Ochs, S. Veitinger, Insook Kim, D. Weiz, A. Angerer, V. Braun
- BiologyMolecular microbiology
- 1 January 1995
In vivo it is reported that in vivo the chromosomally encoded Feel protein activates transcription of the fecA and fecB transport genes in response to ferric citrate and the FecR protein.