Cytoplasmic membrane pathways

Cytoplasmic membrane Polymyxins Polyenes Imidazoles and triazoles Naftidine Disrupt bacterial membranes Disrupt fungal membranes Inhibit ergosterol synthesis Inhibits ergosterol synthesis Bind to LPS and phospholipids Bind preferentially to ergosterol Pathway not in mammalian cells Pathway not in mammalian cells... 

IRON TRANSLOCATION ACROSS THE CYTOPLASMIC MEMBRANE VARIOUS PATHWAYS... 

As described in Section II,A, gram-positive bacteria have only one membrane (the cytoplasmic membrane). Therefore, the translocation through the Sec pathway directly leads proteins to be secreted (Simonen and Palva, 1993 Nagarajan, 1993). The issue of protein sorting into the cell wall is described in a separate section. 

A two-color dot plot (Fig. 8.23) of cells stained with propidium iodide and annexin V FITC will indicate cells in three of the four quadrants. Unstained cells are alive and well and are the double negatives they neither express phosphatidylserine on their surface nor take up propidium iodide through leaky membranes. Cells that stain just with annexin V are apoptotic they have begun to express phosphatidylserine on their surface, but have not yet gone through the process that leads to permeabilization of their cytoplasmic membrane. Cells that stain both with propidium iodide and annexin V are necrotic (that is, dead) they take up propidium iodide and also stain with annexin Y. With a permeable cell, the flow cytometer cannot tell us whether the annexin V is on the outside of the membrane (because the cells have gone through apoptosis before membrane permeabilization) or on the inside of the membrane (because the cells have died by the necrotic pathway without apoptosis). 

Penicillins have been considered for the inhibition of other bacterial serine enzymes than the DD-peptidases and /3-lactamases. For instance, bacterial signal peptidases (SPases) are essential for cell viability and therefore represent nowadays a class of novel antibacterial target <1998NAT186>. SPases are involved in protein translocation through the cytoplasmic membrane in the final step of the bacterial protein secretion pathway <1997PSC1119>. 5(S)-Stereoisomers of penems have been found to inhibit SPases <1995BML443>. The most potent inhibitors are 5/AV-tricyclic penems <2003S1732>. 

The putative pathway of coordination of mannan and PolyP biosynthesis by cell-wall formation has been proposed (Kulaev, 1994), which explains the presence of PolyP outside of the cytoplasmic membrane (Figure 7.4). Dolichyl-phosphates (Dol-Ps) act as transmembrane carriers of carbohydrate residues in glycoprotein biosynthesis. GDP-mannose at the... 

Many biochemical signaling processes involve the coupled reaction diffusion of two or more substrates. Metabolic biochemical pathways are mainly multicomponent reaction cycles leading to binding and/or signaling and are coupled to the transport of substrates. A reaction-diffusion model can also describe the diffusion of certain proteins along the bacterium and their transfer between the cytoplasmic membrane and cytoplasm, and the generation of protein oscillation along the bacterium (Wood and Whitaker, 2000). 

The rest of the known sequences of all four classes of BCB domain-containing proteins feature signal peptides in their precursors, indicating that they are translocated across the bacterial cytoplasmic membrane or are translated on the endoplasmic reticulum-bound ribosomes and sent to the secretory pathway in eukaryotes. Thus they are located in the bacterial periplasm, secreted into the extracellular milieu, or anchored to the cell surface. 

The overall reaction is energy yielding, and allows sufficient ATP production to support reverse electron transport for CO2 fixation. However, the first step, oxidation of NH3 to hydroxylamine, requires the input of reducing power. The second step, hydroxylamine oxidation, yields four electrons. These join the electron transport chain at the level of ubiquinone, from which two are shunted back to AMO for activation of NH3. The N oxidation and electron transport pathways in Nitrosomonas are linked in the cytoplasmic membrane and periplasmic space detailed information from the N. europaea genome (Chain et al., 2003) is consistent with the previous biochemical characterizations of the system (Whittaker et al., 2000). Depending on conditions (and enhanced at low oxygen concentrations), nitric oxide (NO), nitrous oxide (N2O) and even dinitrogen gas (N2) have been reported as secondary products... 

Several pathways exist in which the metal sensing and the transcriptional regulatory functions are handled by two separate proteins (6, 15). A sensor protein spans the cytoplasmic membrane, senses the amount of metals in the periplasm, and communicates this information to the regulatory protein that is inside of the cell. When the concentration of the appropriate metal reaches critical levels, the internal kinase domain of the sensor protein phosphorylates the cytosolic regulatory protein, which activates it to control transcription. These two-component systems are thought to help protect the periplasm from damage. 

Conclusions reached with isolated chloroplasts cannot be directly generalized to the intact cells. In the intact cells copper will be confronted with the cell wall, cell membrane, and various compartments of the cytoplasm before reaching the chloroplasts. One can therefore expect that action on the chioroplast will follow action on the cellular membrane and perhaps on various cytoplasmic metabolic pathways. Copper may inhibit biochemical pathways at the periphery of the cell, with a greater number of organelles being reached as the concentration increases. 

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