Revisiting the interaction between the chaperone Skp and lipopolysaccharide

Burmann, Björn M. and Holdbrook, Daniel A. and Callon, Morgane and Bond, Peter J. and Hiller, Sebastian . (2015) Revisiting the interaction between the chaperone Skp and lipopolysaccharide. Biophysical journal, 108 (6). pp. 1516-1526.

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Official URL: http://edoc.unibas.ch/dok/A6391015

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The bacterial outer membrane comprises two main classes of components, lipids and membrane proteins. These nonsoluble compounds are conveyed across the aqueous periplasm along specific molecular transport routes: the lipid lipopolysaccharide (LPS) is shuttled by the Lpt system, whereas outer membrane proteins (Omps) are transported by chaperones, including the periplasmic Skp. In this study, we revisit the specificity of the chaperone-lipid interaction of Skp and LPS. High-resolution NMR spectroscopy measurements indicate that LPS interacts with Skp nonspecifically, accompanied by destabilization of the Skp trimer and similar to denaturation by the nonnatural detergent lauryldimethylamine-N-oxide (LDAO). Bioinformatic analysis of amino acid conservation, structural analysis of LPS-binding proteins, and MD simulations further confirm the absence of a specific LPS binding site on Skp, making a biological relevance of the interaction unlikely. Instead, our analysis reveals a highly conserved salt-bridge network, which likely has a role for Skp function.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller)
UniBasel Contributors:Hiller Odermatt, Sebastian
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Biophysical Society
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:13 Dec 2017 14:17
Deposited On:03 Jul 2015 08:53

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