Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis
6 affiliations
- 1FIND, Geneva, Switzerland
- 2The Bacterial Cell Biology, Swammerdam Institute for Life Sciences, University of Amsterdam, Amsterdam, The Netherlands
- 3The Centre for Bacterial Cell Biology, Biosciences Institute, Newcastle University, Newcastle upon Tyne, United Kingdom
- 4SUPA, School of Physics and Astronomy, The University of Edinburgh, Edinburgh, Scotland, United Kingdom
- 5Carl Zeiss Meditec AG, Jena, Germany
- 6MRC Laboratory of Molecular Biology, Structural Studies Division, Cambridge, UK
Abstract
Proteins can diffuse micrometers in seconds, yet bacterial cells are able to maintain stable protein gradients. The best studied bacterial protein gradient is the Min system of Escherichia coli. In rod-shaped bacteria the MinCD proteins prevent formation of minicells by inhibiting FtsZ polymerization close to the cell poles. In E. coli these proteins oscillate between cell poles within a minute, resulting in an increased MinCD concentration at the poles. This oscillation is caused by the interaction between MinD and the protein MinE, which form an ATP-driven reaction-diffusion system, whereby the ATPase MinD cycles between a monomeric cytosolic and a dimeric membrane attached states. Bacillus subtilis also has MinCD, but lacks MinE. In this case MinCD form a static gradient that requires the transmembrane protein MinJ, located at cell poles and cell division sites. A recent reaction-diffusion model was successful in recreating the MinD gradient in B. subtilis, assuming that MinD cycles between cytosol and membrane, like in E. coli. Here we show that the monomeric and dimeric states of B. subtilis MinD have comparable membrane affinities, that MinD interacts with MinJ as a dimer, and that MinJ is not required for membrane localization of MinD. Based on these new findings we tested different models, using kinetic Monte Carlo simulations, and found that a difference in diffusion rate between the monomer and dimer, rather than a difference in membrane affinity, is important for B. subtilis MinCD gradient formation.
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BibTeX
@article{bohorquez2026membrane,
title = {{Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis}},
author = {Laura C. Bohórquez and Henrik Strahl and Davide Marenduzzo and Martin J. Thiele and Frank Bürmann and Leendert Willem Hamoen},
journal = {eLife},
year = {2026},
month = sep,
doi = {10.7554/elife.101520.4},
url = {https://doi.org/10.7554/elife.101520.4},
note = {CC BY},
}
RIS
TY - JOUR
TI - Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis
AU - Laura C. Bohórquez
AU - Henrik Strahl
AU - Davide Marenduzzo
AU - Martin J. Thiele
AU - Frank Bürmann
AU - Leendert Willem Hamoen
PY - 2026
DA - 2026/09/02
JO - eLife
DO - 10.7554/elife.101520.4
UR - https://doi.org/10.7554/elife.101520.4
AB - Proteins can diffuse micrometers in seconds, yet bacterial cells are able to maintain stable protein gradients. The best studied bacterial protein gradient is the Min system of Escherichia coli. In rod-shaped bacteria the MinCD proteins prevent formation of minicells by inhibiting FtsZ polymerization close to the cell poles. In E. coli these proteins oscillate between cell poles within a minute, resulting in an increased MinCD concentration at the poles. This oscillation is caused by the interaction between MinD and the protein MinE, which form an ATP-driven reaction-diffusion system, whereby the ATPase MinD cycles between a monomeric cytosolic and a dimeric membrane attached states. Bacillus subtilis also has MinCD, but lacks MinE. In this case MinCD form a static gradient that requires the transmembrane protein MinJ, located at cell poles and cell division sites. A recent reaction-diffusion model was successful in recreating the MinD gradient in B. subtilis, assuming that MinD cycles between cytosol and membrane, like in E. coli. Here we show that the monomeric and dimeric states of B. subtilis MinD have comparable membrane affinities, that MinD interacts with MinJ as a dimer, and that MinJ is not required for membrane localization of MinD. Based on these new findings we tested different models, using kinetic Monte Carlo simulations, and found that a difference in diffusion rate between the monomer and dimer, rather than a difference in membrane affinity, is important for B. subtilis MinCD gradient formation.
SN - 2050-084X
ER -