Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes
The membrane channel-forming colicin A: synthesis, secretion, structure, action and immunity
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Cited by (88)
Colicin import into E. coli cells: A model system for insights into the import mechanisms of bacteriocins
2014, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Bacteriocins are generally narrow spectrum antibacterial agents with biological activity against closely related species and their genes are localized on transposable elements, plasmids or on the chromosome of the producer's genome. Modes of action range from depolarization of the lipid bilayer membranes [5,6], disruption of cell wall synthesis [7,8], inhibition of protein synthesis or degradation of host nucleic acids [9]. Mechanisms of cellular import are dependent on the target organism; enzymatic colicins that cross two lipid bilayer membranes and the peptidoglycan layer of the periplasmic space have a very different navigation pathway than lantibiotics such as mersacidin, which disrupt cell wall synthesis due to interactions with lipid II on the outside of the cell wall.
Does VDAC insert into membranes in random orientation?
2004, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :As a consequence, it is widely accepted that VDAC inserts itself into planar bilayers in a random orientation (i.e., one channel opening does not preferentially face one aqueous compartment). This assertion stands in contrast to the well-documented oriented insertion of channel-forming proteins in planar bilayers [13–19] and to the oriented insertion (into planar lipid bilayer) of purified ion channels normally located in natural membranes [20–23]. Moreover, in many cases, when the authors did not investigate the orientation of the reconstructed porins from different sources, they noted that in response to positive and negative voltage pulses “the current decreased in a somewhat asymmetric fashion which suggested asymmetric insertion of the channels into the membrane” [7,24–26].
Structural investigations of calcium binding and its role in activity and activation of outer membrane phospholipase A from Escherichia coli
2001, Journal of Molecular BiologyCitation Excerpt :Although OMPLA is constitutively expressed in E. coli, no activity is detected under normal conditions.15,16 Activity is observed only after events that disrupt membrane integrity, such as temperature shock, phage-induced lysis, or colicin release.10–13,17,18 A strong induction of OMPLA activity and concomitant extensive breakdown of the outer membrane has lethal consequences for the cell.18
Effects of the antibiotic peptide microcin J25 on liposomes: Role of acyl chain length and negatively charged phospholipid
2000, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :However, a possible effect at the membrane level cannot be discarded due to the high peptide hydrophobicity. In addition, there have been various reports of natural peptides with small molecular weights that induce the permeabilization of membranes, e.g. colicin A [8], magainins [9], nisin [10], bacteriocins [11], sapecins [12], defensins [13] and even some microcins [1,2]. We are interested in the membrane-perturbing ability of MccJ25.
Bacterial phospholipase A: Structure and function of an integral membrane phospholipase
2000, Biochimica et Biophysica Acta - Molecular and Cell Biology of Lipids