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旋转马达蛋白 FF-ATP 合酶对脂质膜的非平衡涨落。

Nonequilibrium fluctuations of lipid membranes by the rotating motor protein FF-ATP synthase.

机构信息

Departamento Química Física I, Universidad Complutense de Madrid, 28040 Madrid, Spain.

Instituto de Investigación Sanitaria Hospital 12 de Octubre (imas12), 28041 Madrid, Spain.

出版信息

Proc Natl Acad Sci U S A. 2017 Oct 24;114(43):11291-11296. doi: 10.1073/pnas.1701207114. Epub 2017 Oct 9.

DOI:10.1073/pnas.1701207114
PMID:29073046
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5664490/
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.

摘要

ATP 合酶是一种旋转的膜蛋白，通过跨膜的质子泵活动合成 ATP。为了揭示这种分子主动泵对其脂质环境弯曲特性的机械影响，我们已经在巨大的单层囊泡中功能重建了 ATP 合酶，并通过闪烁光谱法跟踪膜波动。我们发现，ATP 合酶以约 20Hz 的频率旋转，在脂质囊泡的离散热点处促进大的非平衡变形，从而导致整体膜软化。增强的非平衡波动与通过曲率-蛋白耦合机制在高度弯曲的膜位点处积累活性蛋白是一致的，该机制支持旋转的 ATP 合酶在脂质膜中出现集体效应。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/2e838bb9a2b9/pnas.1701207114fig05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/17ca1e7cf86a/pnas.1701207114sfig01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/f70ac4992e86/pnas.1701207114sfig02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/8d1e7283f027/pnas.1701207114sfig03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/d5380914a9c0/pnas.1701207114fig01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/c04de710816b/pnas.1701207114sfig04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/9c343f13953f/pnas.1701207114sfig05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/e4ad5345458b/pnas.1701207114sfig06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/035a7b5237df/pnas.1701207114sfig07.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/00de3f61612d/pnas.1701207114fig02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/ff660bceff26/pnas.1701207114sfig08.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/e5c2db2245c5/pnas.1701207114fig03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/b82d7a089dca/pnas.1701207114fig04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/2e838bb9a2b9/pnas.1701207114fig05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/17ca1e7cf86a/pnas.1701207114sfig01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/f70ac4992e86/pnas.1701207114sfig02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/8d1e7283f027/pnas.1701207114sfig03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/d5380914a9c0/pnas.1701207114fig01.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/c04de710816b/pnas.1701207114sfig04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/9c343f13953f/pnas.1701207114sfig05.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/e4ad5345458b/pnas.1701207114sfig06.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/035a7b5237df/pnas.1701207114sfig07.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/00de3f61612d/pnas.1701207114fig02.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/ff660bceff26/pnas.1701207114sfig08.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/e5c2db2245c5/pnas.1701207114fig03.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/b82d7a089dca/pnas.1701207114fig04.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/79d5/5664490/2e838bb9a2b9/pnas.1701207114fig05.jpg

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