Publications by authors named "Adrian Merino-Salomon"

The bottom-up reconstitution of proteins for their modular engineering into synthetic cellular systems can reveal hidden protein functions in vitro. This is particularly evident for the bacterial Min proteins, a paradigm for self-organizing reaction-diffusion systems that displays an unexpected functionality of potential interest for bioengineering: the directional active transport of any diffusible cargo molecule on membranes. Here, the MinDE protein system is reported as a versatile surface patterning tool for the rational design of synthetically assembled 3D systems.

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Article Synopsis
  • Liquid-liquid phase separation is crucial for organizing cell interiors, but the relationship between protein condensates and lipid membranes is not well understood.
  • This study focuses on the bacterial nucleoid occlusion protein Noc, revealing that its phase separation is regulated by binding to CTP, a nucleoside triphosphate.
  • The research proposes a model where Noc's ability to form condensates on membranes plays a role in recruiting other proteins like FtsZ, indicating a complex interplay between protein condensation and membrane dynamics.
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Article Synopsis
  • - This research focuses on creating basic machinery for synthetic cells to autonomously divide, inspired by the division process in E. coli using the MinCDE protein system.
  • - The study successfully reconstructs this machinery in lipid vesicles, showcasing the real-time processes of FtsZ filament formation, ring assembly, and subsequent constriction that changes the vesicle shape.
  • - Key experimental factors like macromolecular crowding are emphasized, and the findings may advance the development of synthetic cells capable of self-division.
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Self-organized protein patterns are of tremendous importance for biological decision-making processes. Protein patterns have been shown to identify the site of future cell division, establish cell polarity, and organize faithful DNA segregation. Intriguingly, several key concepts of pattern formation and regulation apply to a variety of different protein systems.

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FtsZ is a key component in bacterial cell division, being the primary protein of the presumably contractile Z ring. In vivo and in vitro, it shows two distinctive features that could so far, however, not be mechanistically linked: self-organization into directionally treadmilling vortices on solid supported membranes, and shape deformation of flexible liposomes. In cells, circumferential treadmilling of FtsZ was shown to recruit septum-building enzymes, but an active force production remains elusive.

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The geometry of reaction compartments can affect the local outcome of interface-restricted reactions. Giant unilamellar vesicles (GUVs) are commonly used to generate cell-sized, membrane-bound reaction compartments, which are, however, always spherical. Herein, we report the development of a microfluidic chip to trap and reversibly deform GUVs into cigar-like shapes.

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