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Mutual Dependence between Membrane Phase Separation and Bacterial Division Protein Dynamics in Synthetic Cell Models.

  • Published In: Angewandte Chemie International Edition, 2025, v. 64, n. 6. P. 1 1 of 3

  • Database: Academic Search Ultimate 2 of 3

  • Authored By: Kanwa, Nishu; Kohyama, Shunshi; Fröhlich, Leonard; Desai, Amogh; Schwille, Petra 3 of 3

Abstract

Cell membranes in bacteria are laterally polarized to produce specific environments for membrane proteins, e.g. proteins involved in cell division which accumulate at mid‐cell or the cell poles. An interesting result of such membrane‐lipid interplay is the reorganization of lipid domains together with membrane‐bound proteins at the onset of cell division, suggesting functional significance of membrane compartments in the cell cycle. Here, by adopting the key bacterial division proteins MinC, MinD, MinE, FtsA and FtsZ as an archetypal spatial patterning system, we present a simple vesicle‐based in vitro model to explore the mutual dependence of protein pattern formation and membrane heterogeneity. Like many other peripheral membrane proteins, Min proteins exhibit preferential binding and macro‐scale pattern formation at Ld domains, which leads to altered oscillation mode selection in phase‐separated membrane compartments (GUVs). Moreover, incorporating bacterial division proteins within phase‐separated GUVs leads to blebbing‐like membrane deformations followed by the reorganization of Lo domains aligning at the neck region of the bleb, which agrees well with the domain rearrangement in bacterial membranes immediately preceding the radial constriction process. Overall, the presented in vitro model system showcases a basic framework to better comprehend the cellular division mechanism in consideration of complex cellular lipid environments. [ABSTRACT FROM AUTHOR]

Additional Information

  • Source:Angewandte Chemie International Edition. 2025/02, Vol. 64, Issue 6, p1
  • Document Type:Article
  • Subject Area:Biology
  • Publication Date:2025
  • ISSN:1433-7851
  • DOI:10.1002/anie.202417800
  • Accession Number:183986216
  • Copyright Statement:Copyright of Angewandte Chemie International Edition is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

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