MurG self-organizes into distinct protein-induced microdomains within fluid lipid membranes
Abstract
Membrane compartmentalization plays a fundamental role in cellular organization, yet the mechanisms underlying it in prokaryotes remain poorly understood. Here, we investigate MurG, an essential membrane-associated N-acetylglucosamine transferase involved in peptidoglycan biosynthesis and conserved across Gram-positive and Gram-negative bacteria. Combining theoretical thermodynamic modeling with experimental high-speed atomic force and fluorescence microscopy, we show that MurG induces membrane partitions independently of lipid segregation, supporting a mechanism of protein-driven membrane organization. In addition, we show that the lateral mobility and spatial distribution of MurG are strongly influenced by membrane fluidity. These MurG-dependent partitions closely resemble the Regions of Increased Fluidity (RIFs), whose molecular origin had remained unclear. Notably, antibiotics alter MurG domain organization and dynamics, linking membrane partitioning to antibiotic exposure. Altogether, our findings reveal a close interplay between protein clustering, membrane dynamics, and lipid bilayer physical properties, providing new insights into the mechanisms underlying membrane compartmentalization in bacteria.
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BibTeX
@misc{lafargue2026murg,
title = {{MurG self-organizes into distinct protein-induced microdomains within fluid lipid membranes}},
author = {Elodie Lafargue and Carlos Marcuello and Thomas M Wood and Nathaniel I Martin and Adai Colom and Marcelo E Guerin and Ignacio Casuso},
howpublished = {HAL},
year = {2026},
month = nov,
url = {https://hal.science/hal-05854738v1},
note = {CC BY-NC 4.0},
}
RIS
TY - UNPB
TI - MurG self-organizes into distinct protein-induced microdomains within fluid lipid membranes
AU - Elodie Lafargue
AU - Carlos Marcuello
AU - Thomas M Wood
AU - Nathaniel I Martin
AU - Adai Colom
AU - Marcelo E Guerin
AU - Ignacio Casuso
PY - 2026
DA - 2026/11/06
PB - HAL
UR - https://hal.science/hal-05854738v1
AB - Membrane compartmentalization plays a fundamental role in cellular organization, yet the mechanisms underlying it in prokaryotes remain poorly understood. Here, we investigate MurG, an essential membrane-associated N-acetylglucosamine transferase involved in peptidoglycan biosynthesis and conserved across Gram-positive and Gram-negative bacteria. Combining theoretical thermodynamic modeling with experimental high-speed atomic force and fluorescence microscopy, we show that MurG induces membrane partitions independently of lipid segregation, supporting a mechanism of protein-driven membrane organization. In addition, we show that the lateral mobility and spatial distribution of MurG are strongly influenced by membrane fluidity. These MurG-dependent partitions closely resemble the Regions of Increased Fluidity (RIFs), whose molecular origin had remained unclear. Notably, antibiotics alter MurG domain organization and dynamics, linking membrane partitioning to antibiotic exposure. Altogether, our findings reveal a close interplay between protein clustering, membrane dynamics, and lipid bilayer physical properties, providing new insights into the mechanisms underlying membrane compartmentalization in bacteria.
ER -