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A programmable DNA-origami platform for studying lipid transfer between bilayers.

Xin Bian1,2,3,4, Zhao Zhang1,5,6, Qiancheng Xiong1,5

  • 1Department of Cell Biology, Yale University School of Medicine, New Haven, CT, USA.

Nature Chemical Biology
|July 20, 2019
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Summary
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Researchers used DNA nanostructures to precisely position liposomes and study lipid transfer by the extended synaptotagmin 1 (E-Syt1) protein. This revealed lipid transport occurs over distances greater than the protein dimer length, supporting a shuttle model.

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Area of Science:

  • Cell Biology
  • Biophysics
  • Nanotechnology

Background:

  • Non-vesicular lipid transport at membrane contact sites is crucial for cellular function.
  • Understanding the precise distances at which lipid transfer proteins operate is key to elucidating their mechanisms.
  • Extended synaptotagmin 1 (E-Syt1) is a key protein involved in tethering and lipid transfer at membrane contact sites.

Purpose of the Study:

  • To determine the functional distance range of lipid transfer mediated by the synaptotagmin-like mitochondrial lipid-binding protein (SMP) domain of E-Syt1.
  • To develop a novel nanotechnological approach for precisely controlling inter-bilayer distances in model membrane systems.
  • To investigate the mechanism of lipid transfer by E-Syt1, specifically testing the shuttle model.

Main Methods:

  • Development of DNA-origami nanostructures to create size-defined donor and acceptor liposomes docked at precise distances via DNA pillars.
  • Anchoring of the SMP domain of E-Syt1 to donor liposomes using an unstructured linker.
  • Quantification of lipid transfer using a Förster resonance energy transfer (FRET)-based assay.

Main Results:

  • Lipid transfer by the SMP domain of E-Syt1 was demonstrated to occur effectively over distances exceeding the length of an SMP dimer.
  • The observed lipid transfer distances are consistent with the predictions of the shuttle model for lipid transport.
  • The developed DNA nanostructures provide a versatile platform for studying membrane-associated protein functions at controlled inter-membrane distances.

Conclusions:

  • The study provides mechanistic insights into E-Syt1 function, supporting a model where the protein facilitates lipid transfer across significant inter-bilayer gaps.
  • The novel DNA-origami based platform enables precise spatial control for studying membrane contact site biology.
  • This methodology can be extended to investigate other protein-mediated interactions occurring at closely apposed membranes.