Interactions between folding factors and bacterial outer membrane proteins
نویسندگان
چکیده
منابع مشابه
Interaction between bacterial outer membrane proteins and periplasmic quality control factors: a kinetic partitioning mechanism.
The OMPs (outer membrane proteins) of Gram-negative bacteria have to be translocated through the periplasmic space before reaching their final destination. The aqueous environment of the periplasmic space and high permeability of the outer membrane engender such a translocation process inevitably challenging. In Escherichia coli, although SurA, Skp and DegP have been identified to function in t...
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The outer membrane (OM) of Gram-negative bacteria is composed of phospholipids in the periplasmic leaflet and lipopolysaccharides (LPS) in the external leaflet, along with β-barrel OM proteins (OMPs) and lipidated periplasmic lipoproteins. As a defensive barrier to toxic compounds, an LPS molecule has high antigenic diversity and unique combination of OM-anchored lipid A with core oligosacchari...
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Surface display of heterologous proteins or polypeptides on the surface of bacteria has gained momentum in recent years. Until recently, arrays of anchors or carriers have been identified for displaying diverse passenger proteins on the surface of Escherichia coli, majority of these involving the outer membrane proteins (OMPs). The reason for opting outer membrane proteins lies mainly i n its a...
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Isolation and purification of major outer membrane proteins (OMP) from the cell wall envelope of Brucella abortus S-99 were achieved by sonication, solubilization and membrane fractionation in the presence of non-ionic detergent (Tx-100) and lysozyme treatments, followed by ultracentrifugation. The crude OMP was treated with trypsin to free the preparation from any other protein contaminan...
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Membrane proteins can deform the lipid bilayer in which they are embedded. If the bilayer is treated as an elastic medium, then these deformations will generate elastic interactions between the proteins. The interaction between a single pair is repulsive. However, for three or more proteins, we show that there are nonpairwise forces whose magnitude is similar to the pairwise forces. When there ...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2005
ISSN: 0950-382X
DOI: 10.1111/j.1365-2958.2005.04674.x