Protein‐Assisted Large‐Scale Assembly and Differential Patterning of DNA Origami Lattices

Abstract

Nanofabrication has experienced a big boost with the invention of DNA origami, enabling the production and assembly of complex nanoscale structures that may be able to unlock fully new functionalities in biology and beyond. The remarkable precision with which these structures can be designed and produced is, however, not yet matched by their assembly dynamics, which can be extremely slow, particularly when attached to biological templates, such as membranes. Here, the rapid and controlled formation of DNA origami lattices on the scale of hundreds of micrometers in as little as 30 minutes is demonstrated, utilizing active patterning by the E.coli Min protein system, thereby yielding a remarkable improvement over conventional passive diffusion‐based assembly methods. Various patterns, including spots, inverse spots, mazes, and meshes can be produced at different scales, tailored through the shape and density of the assembled structures. The differential positioning accomplished by Min‐induced diffusiophoresis even allows the introduction of “pseudo‐colors”, i.e., complex core–shell patterns, by simultaneously patterning different DNA origami species. Beyond the targeted functionalization of biological surfaces, this approach may also be promising for applications in plasmonics, catalysis, and molecular sensing.

Self-organized spatial targeting of contractile actomyosin rings for synthetic cell division

“…16 This newly discovered biochemical function, although possibly irrelevant in vivo, could thus be exploited for the positioning of membraneattached molecules and other biomimetic features in artificial systems. 17,18 In this study, we demonstrate the successful co-reconstitution of actomyosin architectures and the MinDE system inside GUVs. Upon optimization of encapsulation conditions, time-lapse imaging revealed the MinDE-driven diffusiophoretic positioning of actomyosin rings and bundle networks at mid-cell, where we observed equatorial furrow-like invaginations breaking spherical symmetry.…”

“…10 Interestingly, recent studies have shown the robustness and versatility of a protein-based spatial positioning toolset: the MinDE system. [16][17][18] The Escherichia coli (E. coli) Min proteins are a reaction-diffusion system able to self-organize on membranes through ATP hydrolysis.…”

“…Interestingly, recent studies have shown the robustness and versatility of a protein-based spatial positioning toolset: the MinDE system. 16–18 The Escherichia coli ( E. coli ) Min proteins are a reaction-diffusion system able to self-organize on membranes through ATP hydrolysis. Composed of three proteins – MinD, MinE and MinC – the Min complex has a particular function in vivo : the localization of the FtsZ division ring (Z-ring) in the middle of rod-shape bacteria.…”

“…16 This newly discovered biochemical function, although possibly irrelevant in vivo , could thus be exploited for the positioning of membrane-attached molecules and other biomimetic features in artificial systems. 17,18…”