article · 10/10/2017
Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F1F0-ATP synthase
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Résumé
ATP synthase is a rotating membrane protein that synthesizes ATP through proton-pumping activity across the membrane. To unveil the mechanical impact of this molecular active pump on the bending properties of its lipid environment, we have functionally reconstituted the ATP synthase in giant unilamellar vesicles and tracked the membrane fluctuations by means of flickering spectroscopy. We find that ATP synthase rotates at a frequency of about 20 Hz, promoting large nonequilibrium deformations at discrete hot spots in lipid vesicles and thus inducing an overall membrane softening. The enhanced nonequilibrium fluctuations are compatible with an accumulation of active proteins at highly curved membrane sites through a curvature-protein coupling mechanism that supports the emergence of collective effects of rotating ATP synthases in lipid membranes.
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Almendro-Vedia, V.-G., Natale, P., Mell, M., Bonneau, S., Monroy, F., Joubert, F., & López-Montero, I. (2017). Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F1F0-ATP synthase. Proceedings of the National Academy of Sciences of the United States of America. https://doi.org/10.1073/pnas.1701207114@article{AlmendroVedia2017_161,
author = {Almendro-Vedia, Víctor G. and Natale, Paolo and Mell, Michael and Bonneau, Stephanie and Monroy, Francisco and Joubert, Frederic and López-Montero, Iván},
year = {2017},
month = {10},
title = {Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F1F0-ATP synthase},
journal = {Proceedings of the National Academy of Sciences of the United States of America},
abstract = {ATP synthase is a rotating membrane protein that synthesizes ATP through proton-pumping activity across the membrane. To unveil the mechanical impact of this molecular active pump on the bending properties of its lipid environment, we have functionally reconstituted the ATP synthase in giant unilamellar vesicles and tracked the membrane fluctuations by means of flickering spectroscopy. We find that ATP synthase rotates at a frequency of about 20 Hz, promoting large nonequilibrium deformations at discrete hot spots in lipid vesicles and thus inducing an overall membrane softening. The enhanced nonequilibrium fluctuations are compatible with an accumulation of active proteins at highly curved membrane sites through a curvature-protein coupling mechanism that supports the emergence of collective effects of rotating ATP synthases in lipid membranes.},
url = {http://www.pnas.org/content/early/2017/10/03/1701207114.abstract?sid=9ef323ac-d756-48b9-be87-3b8b21483900},
doi = {10.1073/pnas.1701207114},
}TY - JOUR
AU - Almendro-Vedia, Víctor G.
AU - Natale, Paolo
AU - Mell, Michael
AU - Bonneau, Stephanie
AU - Monroy, Francisco
AU - Joubert, Frederic
AU - López-Montero, Iván
PY - 2017
DA - 2017/10/10
TI - Nonequilibrium fluctuations of lipid membranes by the rotating motor protein F1F0-ATP synthase
JO - Proceedings of the National Academy of Sciences of the United States of America
AB - ATP synthase is a rotating membrane protein that synthesizes ATP through proton-pumping activity across the membrane. To unveil the mechanical impact of this molecular active pump on the bending properties of its lipid environment, we have functionally reconstituted the ATP synthase in giant unilamellar vesicles and tracked the membrane fluctuations by means of flickering spectroscopy. We find that ATP synthase rotates at a frequency of about 20 Hz, promoting large nonequilibrium deformations at discrete hot spots in lipid vesicles and thus inducing an overall membrane softening. The enhanced nonequilibrium fluctuations are compatible with an accumulation of active proteins at highly curved membrane sites through a curvature-protein coupling mechanism that supports the emergence of collective effects of rotating ATP synthases in lipid membranes.
DO - 10.1073/pnas.1701207114
UR - http://www.pnas.org/content/early/2017/10/03/1701207114.abstract?sid=9ef323ac-d756-48b9-be87-3b8b21483900
ER -