Lipid-dependent membrane protein

Lipid-surfactant mixtures have gained much interest in context with the solubilization of membranes and with the problem of reconstituting membrane proteins into artificial membrane systems such as unilamellar vesicles. For the solubilization of membranes, a sufficiently high concentration of an aqueous micellar solution has to be added to the membrane suspension, so that the bilayers are transformed into mixed micelles containing surfactant, membrane lipids, and membrane proteins. This solubilization process is quite complicated and the necessary amounts of surfactant for complete solubilization depends on the nature of the surfactant, the type of membrane, and the total concentration of lipid and surfactant. 

In series with a desolvation energy barrier required to disrupt aqueous solute hydrogen bonds [14], the lipid bilayer offers a practically impermeable barrier to hydrophilic solutes. It follows that significant transepithelial transport of water-soluble molecules must be conducted paracellularly or mediated by solute translocation via specific integral membrane proteins (Fig. 6). Transcellular permeability of lipophilic solutes depends on their solubility in GI membrane lipids relative to their aqueous solubility. This lumped parameter, membrane permeability,... 

Recent results indicate that not only topogenic signals and membrane composition contribute to the proper topology of a membrane protein. The antimicrobial peptide nisin, produced by Lactococcus lactis, kills Gram-positive bacteria via pore formation, thus leading to the permeabilisation of the membrane. Nisin depends on the cell-wall precursor Lipid II, which functions as a docking molecule to support a perpendicular stable transmembrane orientation [43]. 

Bogdanov, M., Heacock, P. N. and Dowhan, W. (2002). A polytopic membrane protein displays a reversible topology dependent on membrane lipid composition, EMBOJ., 21, 2107-2116. 

The subcellular distribution of lipid-dependent, glycosylation reactions has also been investigated in a number of plant systems. In plant cells, the situation is, however, more complicated, as their membranes often have the capability to transfer activated sugars, not only to lipid-bound saccharides201-203 and to proteins,4B-204-2,)li but also to cell-wall... 

The calcium-independent ATPase of the lipid modified preparations is not only different from the calcium-dependent ATPase but also from the calcium-independent ATPase of native preparations — the basic ATPase — which has a lower nucleotide specificity126. The experiments in which the lipid matrix of the sarcoplasmic membranes has been replaced by lipid compounds not present in native membranes reveal a high degree of functional flexibility of the enzyme. On the other hand, a few residual lipids in the protein are sufficient to prevent these changes in the structure of the enzyme and to preserve its calcium sensitivity. 

Prenylation (covalent attachment of an isoprenoid see Fig. 27-30) is a common mechanism by which proteins are anchored to the inner surface of cellular membranes in mammals (see Fig. 11-14). In some of these proteins the attached lipid is the 15-carbon farnesyl group others have the 20-carbon geranylgeranyl group. Different enzymes attach the two types of lipids. It is possible that prenylation reactions target proteins to different membranes, depending on which lipid is attached. Protein prenylation is another important role for the isoprene derivatives of the pathway to cholesterol. 

Biological membranes are always pictured as being very selective barriers separating different biochemical reaction compartments. This high performance transport specificity solely depends on the presence of membrane proteins embedded in the lipid matrix. On the other hand, most membrane proteins cease to function in the absence of lipids. In order to introduce biological transport abilities into artificial membrane systems protein-lipid interactions are of vital interest. The question is how the activity of membrane proteins is affected if they are placed into a polymeric environment. 

Biological membranes consist primarily of proteins and lip-ids. The relative amounts of these materials vary considerably, depending on the source of the membrane. At one extreme, the inner mitochondrial membrane is about 80% protein and 20% lipid by weight at the other, the myelin sheath membrane is about 80% lipid and 20% protein. The plasma membrane of human erythrocytes contains about equal amounts of protein and lipid. Many membranes also contain small amounts of carbohydrates. These almost always are covalently attached to either proteins (as glycoproteins) or lipids (as glycolipids or lipopolysaccharides). The mitochondrial inner membrane has little or no carbohydrate, but the myelin membrane has about 3% carbohydrate by weight, and the erythrocyte plasma membrane about 8%. 

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