The E. coli MinCDE system in the regulation of protein patterns and gradients

Abstract

Molecular self-organziation, also regarded as pattern formation, is crucial for the correct distribution of cellular content. The processes leading to spatiotemporal patterns often involve a multitude of molecules interacting in complex networks, so that only very few cellular pattern-forming systems can be regarded as well understood. Due to its compositional simplicity, the Escherichia coli MinCDE system has, thus, become a paradigm for protein pattern formation. This biological reaction diffusion system spatiotemporally positions the division machinery in E. coli and is closely related to ParA-type ATPases involved in most aspects of spatiotemporal organization in bacteria. The ATPase MinD and the ATPase-activating protein MinE self-organize on the membrane as a reaction matrix. In vivo, these two proteins typically oscillate from pole-to-pole, while in vitro they can form a variety of distinct patterns. MinC is a passenger protein supposedly operating as a downstream cue of the system, coupling it to the division machinery. The MinCDE system has helped to extract not only the principles underlying intracellular patterns, but also how they are shaped by cellular boundaries. Moreover, it serves as a model to investigate how patterns can confer information through specific and non-specific interactions with other molecules. Here, we review how the three Min proteins self-organize to form patterns, their response to geometric boundaries, and how these patterns can in turn induce patterns of other molecules, focusing primarily on experimental approaches and developments.

Adaptability and evolution of the cell polarization machinery in budding yeast

“…When the phenotype (function) is determined by a self-organized process, the genotype-to-phenotype relation is not a simple one-to-one mapping (or "blueprint"). As a concrete example take intracellular (protein-based) pattern formation, which is essential for many essential cellular functions, like division and motility (Howard et al, 2011;Ramm et al, 2019). The genotype determines the components (proteins), their interaction network and their copy numbers.…”

Integrated Proteomic and Transcriptomic Analyses Reveal the Roles of Brucella Homolog of BAX Inhibitor 1 in Cell Division and Membrane Homeostasis of Brucella suis S2

“…The early (Z-ring) and late divisome components are linked by the FtsQBL complex, which may have a structural role as a scaffold in assembling the divisome ( Choi et al, 2018 ; Condon et al, 2018 ). In most bacteria, to guarantee that division occurs at the correct site, a Min system comprising MinC, MinD, and MinE prevents establishing the divisome at bacterial poles ( Szwedziak and Ghosal, 2017 ; Ramm et al, 2019 ). As a spatial modulator of the divisome, defects in the Min system produce small anucleate minicells from the poles of rod-shaped mother cells, increasing the average cell length of the DNA-containing mother cells ( Lutkenhaus, 2007 ).…”

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

“…Nucleotide hydrolysis leads, in turn, to the detachment of MinD from the lipid membrane, and the continuous cycling of this mechanism gives rise to protein self-organization and pattern formation. 12 , 13 At first, this system might appear complex; however, one can appreciate the distinct output, as pattern formation is only possible if the moieties of interest, fused to the minimal MinE peptide, are able to interact ( Figure 1 d). In contrast, non-interacting moieties result in homogeneous MinD membrane coverage, deficient in ATP hydrolysis.…”