期刊
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
卷 138, 期 13, 页码 4439-4447出版社
AMER CHEMICAL SOC
DOI: 10.1021/jacs.5b13107
关键词
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资金
- US National Institutes of Health (NIH) Grant [DK027044-39]
- Agence Nationale de la Recherche (ANR) [ANR-14-1CHN-0022-01]
- National Institutes of Health (NIH) Director's New Innovator Award [DP2-GM114830, DP2-OD004641]
- NIH grant [R21-GM109466, R01GM108954]
- Yale University faculty startup fund
- Army Research Office MURI grant [W911NF-12-1-0420]
- National Science Foundation Expeditions Grant [1317694]
- Wyss Institute for Biologically Inspired Engineering Faculty Award
- Kavli Neuroscience Scholar Award
- Direct For Computer & Info Scie & Enginr
- Division of Computing and Communication Foundations [1317291] Funding Source: National Science Foundation
- Division of Computing and Communication Foundations
- Direct For Computer & Info Scie & Enginr [1317694] Funding Source: National Science Foundation
Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes are the core molecular machinery of membrane fusion, a fundamental process that drives inter- and intracellular communication and trafficking. One of the questions that remains controversial has been whether and how SNAREs cooperate. Here we show the use of self-assembled DNA-nanostructure rings to template uniform-sized small unilamellar vesicles containing predetermined maximal number of externally facing SNAREs to study the membrane-fusion process. We also incorporated lipid-conjugated complementary ssDNA as tethers into vesicle and target membranes, which enabled bypass of the rate-limiting docking step of fusion reactions and allowed direct observation of individual membrane-fusion events at SNARE densities as low as one pair per vesicle. With this platform, we confirmed at the single event level that, after docking of the templated-SUVs to supported lipid bilayers (SBL), one to two pairs of SNAREs are sufficient to drive fast lipid mixing. Modularity and programmability of this platform makes it readily amenable to studying more complicated systems where auxiliary proteins are involved.
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