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Independent mobility of proteins and lipids in the plasma membrane of <i>E</i><i>scherichia coli</i>
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Independent mobility of proteins and lipids in the plasma membrane of Escherichia coli

Author: Anja Nenninger Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UKGiulia Mastroianni Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UKAlexander Robson Affiliation: Clarendon Laboratory, University of Oxford, Parks Road, Oxford, UKTchern Lenn Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UKQuan Xue Affiliation: Clarendon Laboratory, University of Oxford, Parks Road, Oxford, UKAll authors
Edition/Format: Article Article : English
Publication:Molecular Microbiology, v92 n5 (June 2014): 1142-1153
Summary:
Fluidity is essential for many biological membrane functions. The basis for understanding membrane structure remains the classic Singer-Nicolson model, in which proteins are embedded within a fluid lipid bilayer and able to diffuse laterally within a sea of lipid. Here we report lipid and protein diffusion in the plasma membrane of live cells of the bacterium Escherichia coli, using Fluorescence Recovery after Photobleaching (FRAP) and Total Internal Reflection Fluorescence (TIRF) microscopy to measure lateral diffusion coefficients. Lipid and protein mobility within the membrane were probed by visualizing an artificial fluorescent lipid and a simple model membrane protein consisting of a single membrane-spanning alpha-helix with a Green Fluorescent Protein (GFP) tag on the cytoplasmic side. The effective viscosity of the lipid bilayer is strongly temperature-dependent, as indicated by changes in the lipid diffusion coefficient. Surprisingly, the mobility of the model protein was unaffected by changes in the effective viscosity of the bulk lipid, and TIRF microscopy indicates that it clusters in segregated, mobile domains. We suggest that this segregation profoundly influences the physical behaviour of the protein in the membrane, with strong implications for bacterial membrane function and bacterial physiology.  Read more...
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Document Type: Article
All Authors / Contributors: Anja Nenninger Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UK; Giulia Mastroianni Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UK; Alexander Robson Affiliation: Clarendon Laboratory, University of Oxford, Parks Road, Oxford, UK; Tchern Lenn Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UK; Quan Xue Affiliation: Clarendon Laboratory, University of Oxford, Parks Road, Oxford, UK; Mark C Leake Affiliation: Biological Physical Sciences Institute (BPSI), University of York, York, UK; Conrad W Mullineaux Affiliation: School of Biological and Chemical Sciences, Queen Mary University of London, Mile End Road, London, UK
ISSN:0950-382X
Language Note: English
Unique Identifier: 5585895482
Notes: For correspondence. E-mail c.mullineaux@qmul.ac.uk; Tel. (+44) 20 7882 3645; Fax (+44) 20 7882 7427.
Awards:
Other Titles: Protein diffusion in a bacterial plasma membrane
Responsibility: A. Nenninger et al.

Abstract:

Fluidity is essential for many biological membrane functions. The basis for understanding membrane structure remains the classic Singer-Nicolson model, in which proteins are embedded within a fluid lipid bilayer and able to diffuse laterally within a sea of lipid. Here we report lipid and protein diffusion in the plasma membrane of live cells of the bacterium Escherichia coli, using Fluorescence Recovery after Photobleaching (FRAP) and Total Internal Reflection Fluorescence (TIRF) microscopy to measure lateral diffusion coefficients. Lipid and protein mobility within the membrane were probed by visualizing an artificial fluorescent lipid and a simple model membrane protein consisting of a single membrane-spanning alpha-helix with a Green Fluorescent Protein (GFP) tag on the cytoplasmic side. The effective viscosity of the lipid bilayer is strongly temperature-dependent, as indicated by changes in the lipid diffusion coefficient. Surprisingly, the mobility of the model protein was unaffected by changes in the effective viscosity of the bulk lipid, and TIRF microscopy indicates that it clusters in segregated, mobile domains. We suggest that this segregation profoundly influences the physical behaviour of the protein in the membrane, with strong implications for bacterial membrane function and bacterial physiology.

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