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Gröger, T. ; Nathoo, S.* ; Ku, T.* ; Sikora, C.* ; Turner, R.J.* ; Prenner, E.J.*

Real-time imaging of lipid domains and distinct coexisting membrane protein clusters.

Chem. Phys. Lipids 165, 216-224 (2012)
DOI PMC
Open Access Green as soon as Postprint is submitted to ZB.
A detailed understanding of biomembrane architecture is still a challenging task. Many in vitro studies have shown lipid domains but much less information is known about the lateral organization of membrane proteins because their hydrophobic nature limits the use of many experimental methods. We examined lipid domain formation in biomimetic Escherichia coli membranes composed of phosphatidylethanolamine and phosphatidylglycerol in the absence and presence of 1% and 5% (mol/mol) membrane multidrug resistance protein, EmrE. Monolayer isotherms demonstrated protein insertion into the lipid monolayer. Subsequently, Brewster angle microscopy was applied to image domains in lipid matrices and lipid-protein mixtures. The images showed a concentration dependent impact of the protein on lipid domain size and shape and more interestingly distinct coexisting protein clusters. Whereas lipid domains varied in size (14-47μm), protein clusters exhibited a narrow size distribution (2.6-4.8μm) suggesting a non-random process of cluster formation. A 3-D display clearly indicates that these proteins clusters protrude from the membrane plane. These data demonstrate distinct co-existing lipid domains and membrane protein clusters as the monofilm is being compressed and illustrate the significant mutual impact of lipid-protein interactions on lateral membrane architecture.
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Publication type Article: Journal article
Document type Scientific Article
Corresponding Author
Keywords Monolayer; Phospholipids; Membrane protein; E. coli; EmrE; Brewster angle microscopy
ISSN (print) / ISBN 0009-3084
e-ISSN 0009-3084
Journal Chemistry and Physics of Lipids
Quellenangaben Volume: 165, Issue: 2, Pages: 216-224 Article Number: , Supplement: ,
Publisher Elsevier
Non-patent literature Publications
Reviewing status Peer reviewed
Institute(s) Cooperation Group Comprehensive Molecular Analytics (CMA)