Optical Control of a Biological Reaction–Diffusion System

Abstract

Patterns formed by reaction and diffusion are the foundation for many phenomena in biology.H owever,t he experimental study of reaction-diffusion (R-D) systems has so far been dominated by chemical oscillators,f or whichm any tools are available.I nt his work, we developed ap hotoswitch for the Min system of Escherichia coli, av ersatile biological in vitro R-D system consisting of the antagonistic proteins MinD and MinE. AM inE-derived peptide of 19 amino acids was covalently modified with aphotoisomerizable crosslinker based on azobenzene to externally control peptide-mediated depletion of MinD from the membrane.I na ddition to providing an on-off switch for pattern formation, we achieve frequency-locked resonance with aprecise 2D spatial memory, thus allowing new insights into Min protein action on the membrane.T aken together,w ep rovide at ool to study phenomena in pattern formation using biological agents.

Probing Biomolecular Interactions by a Pattern-Forming Peptide–Conjugate Sensor

“…The first functional element of our assay system is a short α-helical sequence (aa 13–31) derived from E. coli MinE, which is essential for the stimulation of MinD ATPase activity. 6 , 10 As MinD is only stimulated by dimers of MinE bearing two copies of said α-helical peptide, the second functional element is a pair of interacting moieties ( Figure 1 a). Potentially any type of peptide-conjugated biomolecule can be used to drive dimerization of the minimal MinE peptide ( Figure 1 c).…”

“…In particular, the ATPase-activating protein MinE has been the target of several mutation studies to understand the structure–function relationship of its domains and has recently been successfully reduced to a minimal, pattern-inducing entity. 6 , 9 , 10 MinE comprises four functional motifs: a membrane targeting sequence (MTS), a conformational switch enabling the exchange of an open (active) and a closed (inactive) arrangement, a dimerization interface, and a short α-helical peptide that activates MinD ATPase activity. 6 , 10 , 11 Intriguingly, the ATPase-activating peptide in combination with either the MTS or any moiety capable of dimerization is sufficient to induce MinD pattern formation.…”

“… 6 , 9 , 10 MinE comprises four functional motifs: a membrane targeting sequence (MTS), a conformational switch enabling the exchange of an open (active) and a closed (inactive) arrangement, a dimerization interface, and a short α-helical peptide that activates MinD ATPase activity. 6 , 10 , 11 Intriguingly, the ATPase-activating peptide in combination with either the MTS or any moiety capable of dimerization is sufficient to induce MinD pattern formation. 6 It is thus tempting to extrapolate the functionality of dimerization even beyond the protein context.…”

Lebensfunktionen neu erdacht

“…Ausgehend von diesem gut erforschten und im Labor etablierten System hat Schwilles Arbeitsgruppe nun damit begonnen, neue Funktionalitäten – ohne natürliches Vorbild – einzuführen. Ihr Team baute in das System einen Schalter ein, der es ermöglicht, die Selbstorganisation durch Lichteinstrahlung zu aktivieren (Abbildung ) .…”

In vitro reconstitution of the bacterial cytoskeleton: expected and unexpected new insights

“…Finally, bacterial cytoskeletal components may be engineered and employed in a new context towards the bottom‐up construction of artificial cells. One example is the recent development of a photoswitchable MinDE system to control pattern formation (Glock et al ., ). Additionally, how the self‐organizing properties of the bacterial cytoskeleton can be diverted towards new use was lately demonstrated using the polymeric features of FtsZ.…”