Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes

Murat Tutus; Fernanda F Rossetti; Emanuel Schneck; Giovanna Fragneto; Friedrich Förster; Ralf Richter; Thomas Nawroth; Motomu Tanaka

doi:10.1002/mabi.200800128

Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes

Murat Tutus, Fernanda F Rossetti, Emanuel Schneck, Giovanna Fragneto, Friedrich Förster, Ralf Richter, Thomas Nawroth, Motomu Tanaka

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Research output: Contribution to journal › Article › Academic › peer-review

Abstract

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.

Original language	English
Pages (from-to)	1034-43
Number of pages	10
Journal	Macromolecular Bioscience
Volume	8
Issue number	11
DOIs	https://doi.org/10.1002/mabi.200800128
Publication status	Published - 10 Nov 2008
Externally published	Yes

Keywords

Liposomes
Membranes, Artificial
Micrococcus luteus
Models, Biological
Proton-Translocating ATPases
Surface-Active Agents

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10.1002/mabi.200800128

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title = "Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes",

abstract = "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.",

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author = "Murat Tutus and Rossetti, {Fernanda F} and Emanuel Schneck and Giovanna Fragneto and Friedrich F{\"o}rster and Ralf Richter and Thomas Nawroth and Motomu Tanaka",

year = "2008",

month = nov,

day = "10",

doi = "10.1002/mabi.200800128",

language = "English",

volume = "8",

pages = "1034--43",

journal = "Macromolecular Bioscience",

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publisher = "Wiley-VCH Verlag",

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TY - JOUR

T1 - Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes

AU - Tutus, Murat

AU - Rossetti, Fernanda F

AU - Schneck, Emanuel

AU - Fragneto, Giovanna

AU - Förster, Friedrich

AU - Richter, Ralf

AU - Nawroth, Thomas

AU - Tanaka, Motomu

PY - 2008/11/10

Y1 - 2008/11/10

N2 - 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.

AB - 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.

KW - Liposomes

KW - Membranes, Artificial

KW - Micrococcus luteus

KW - Models, Biological

KW - Proton-Translocating ATPases

KW - Surface-Active Agents

U2 - 10.1002/mabi.200800128

DO - 10.1002/mabi.200800128

M3 - Article

C2 - 18683168

SN - 1616-5187

VL - 8

SP - 1034

EP - 1043

JO - Macromolecular Bioscience

JF - Macromolecular Bioscience

IS - 11

ER -

Orientation-selective incorporation of transmembrane F0F1 ATP synthase complex from micrococcus luteus in polymer-supported membranes

Abstract

Keywords

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