Revisiting the Interaction between the Chaperone Skp and Lipopolysaccharide

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 membran...

Full description

Saved in:
Bibliographic Details
Published in:Biophysical journal 2015-03, Vol.108 (6), p.1516-1526
Main Authors: Burmann, Björn M., Holdbrook, Daniel A., Callon, Morgane, Bond, Peter J., Hiller, Sebastian
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Binding Sites
Biophysics
Detergents - chemistry
Dimethylamines - chemistry
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - genetics
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Lipids
Lipopolysaccharides - chemistry
Membranes
Molecular Chaperones - chemistry
Molecular Chaperones - genetics
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular
Protein Conformation
Protein Denaturation - drug effects
Protein Multimerization - drug effects
Proteins
Proteins and Nucleic Acids
Simulation
Spectrum analysis
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0006-3495
1542-0086
DOI:10.1016/j.bpj.2015.01.029