Tuning membrane protein mobility by confinement into nanodomains
Publikation, 2016
Outline
A. Karner, B. Nimmervoll, B. Plochberger, E. Klotzsch, A. Horner, D. Knyazev, R. Kuttner, K. Winkler, L. Winter, C. Siligan, N. Ollinger, P. Pohl, J. Preiner - Tuning membrane protein mobility by confinement into nanodomains - Nature Nanotechnology, Vol. 12, No. 3, 2016
Abstract
High-speed atomic force microscopy (HS-AFM) can be used to visualize function-related conformational changes of single
soluble proteins. Similar studies of single membrane proteins are, however, hampered by a lack of suitable flat, noninteracting
membrane supports and by high protein mobility. Here we show that streptavidin crystals grown on micasupported
lipid bilayers can be used as porous supports for membranes containing biotinylated lipids. Using SecYEG
(protein translocation channel) and GlpF (aquaglyceroporin), we demonstrate that the platform can be used to tune the
lateral mobility of transmembrane proteins to any value within the dynamic range accessible to HS-AFM imaging through
glutaraldehyde-cross-linking of the streptavidin. This allows HS-AFM to study the conformation or docking of spatially
confined proteins, which we illustrate by imaging GlpF at sub-molecular resolution and by observing the motor protein
SecA binding to SecYEG.
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