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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.

Authors+Show Affiliations

Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany.Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152, Martinsried, Germany. schwille@biochem.mpg.de.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

31317204

Citation

Ramm, Beatrice, et al. "The E. Coli MinCDE System in the Regulation of Protein Patterns and Gradients." Cellular and Molecular Life Sciences : CMLS, 2019.
Ramm B, Heermann T, Schwille P. The E. coli MinCDE system in the regulation of protein patterns and gradients. Cell Mol Life Sci. 2019.
Ramm, B., Heermann, T., & Schwille, P. (2019). The E. coli MinCDE system in the regulation of protein patterns and gradients. Cellular and Molecular Life Sciences : CMLS, doi:10.1007/s00018-019-03218-x.
Ramm B, Heermann T, Schwille P. The E. Coli MinCDE System in the Regulation of Protein Patterns and Gradients. Cell Mol Life Sci. 2019 Jul 17; PubMed PMID: 31317204.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The E. coli MinCDE system in the regulation of protein patterns and gradients. AU - Ramm,Beatrice, AU - Heermann,Tamara, AU - Schwille,Petra, Y1 - 2019/07/17/ PY - 2019/04/30/received PY - 2019/07/02/accepted PY - 2019/06/27/revised PY - 2019/7/19/entrez KW - FtsZ KW - Geometry sensing KW - ParA-type ATPase KW - Reaction–diffusion mechanism KW - Reconstitution KW - Spatiotemporal regulation JF - Cellular and molecular life sciences : CMLS JO - Cell. Mol. Life Sci. N2 - 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. SN - 1420-9071 UR - https://www.unboundmedicine.com/medline/citation/31317204/The_E._coli_MinCDE_system_in_the_regulation_of_protein_patterns_and_gradients L2 - https://dx.doi.org/10.1007/s00018-019-03218-x DB - PRIME DP - Unbound Medicine ER -