Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes.
We report the vectorial incorporation of a highly asymmetric F0F1 ATP synthase complex from Micrococcus luteus into polymer-supported membranes. Dynamic light scattering and cryo electron microscopy confirm that the use of weak surfactants (bile acid) allows for the non-disruptive protein incorporation into lipid vesicles. Spreading of vesicles with ATP synthase onto a cellulose support results in a homogeneous distribution of proteins, in contrast to a patchy image observed on bare glass slides. The orientation of ATP synthase can be identified using an antibody to the ATP binding site as well as from topographic profiles of the surface. The method to "align" transmembrane proteins in supported membranes would open a possibility to quantify protein functions in biomimetic model systems.
Tutus
Murat
M
Biophysical Chemistry Laboratory and Center for Quantitative Biology (BIOQUANT), University of Heidelberg, 69120 Heidelberg, Germany.
Rossetti
Fernanda F
FF
Schneck
Emanuel
E
Fragneto
Giovanna
G
Förster
Friedrich
F
Richter
Ralf
R
Nawroth
Thomas
T
Tanaka
Motomu
M
D008081:Liposomes; D008567:Membranes, Artificial; D016982:Micrococcus luteus / Q000201:enzymology; D008954:Models, Biological; D006180:Proton-Translocating ATPases / Q000737:chemistry*; D013501:Surface-Active Agents
D008081:Liposomes; D008567:Membranes, Artificial; D013501:Surface-Active Agents; D006180:Proton-Translocating ATPases