5 The membrane can thus be considered as a catalyst for Min pattern formation. ![]() During membrane binding, the diffusion constants of the proteins are locally decreased, inducing dynamic instability as needed to form the self-organized patterns. 4 Importantly, MinD and full-length MinE need to interact with phospholipid membranes for pattern formation. MinE exhibits a latent cytosolic conformation and an active conformation in the presence of membrane-bound MinD, which induces MinE recruitment to the membrane, ATP hydrolysis in MinD, and subsequent dissociation of MinD and MinE from the membrane. Upon ATP binding and dimerization, MinD gains sufficiently high affinity to bind the membrane via the simultaneous presence of two individually weak membrane targeting sequences (MTS). MinD is an ATPase that dimerizes in its ATP-bound state. 3 MinD, MinE and ATP are necessary and sufficient to form Min patterns on lipid membranes. coli cell, regulating the position of the FtsZ ring that orchestrates cell division. The Min proteins oscillate from pole-to-pole within the rod-shaped E. ![]() ![]() coli) Min system has been extensively studied in vivo, in vitro, and in silico, and has become a model system for protein pattern formation. Because of its compositional simplicity, the Escherichia coli ( E. 1 One paradigmatic feature of self-organization is pattern formation that can be found throughout all kingdoms of life. Self-organization supports morphological changes through energy dissipation, enabling evolutionary adaption to varied environmental conditions and exercise complex tasks characteristic of life. Living systems are based on self-organization, by which the interactions of a system's components generate emergent structures and functions.
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