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The best-studied bacterial protein gradient is the Min system of\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    . In rod-shaped bacteria, the MinCD proteins prevent formation of minicells by inhibiting FtsZ polymerization close to the cell poles. In\n                    <jats:italic>E. coli<\/jats:italic>\n                    , 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 state.\n                    <jats:italic>Bacillus subtilis<\/jats:italic>\n                    also has MinCD, but lacks MinE. In this case, MinCD forms 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\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    , assuming that MinD cycles between cytosol and membrane, like in\n                    <jats:italic>E. coli<\/jats:italic>\n                    . Here, we show that the monomeric and dimeric states of\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    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\n                    <jats:italic>B. subtilis<\/jats:italic>\n                    MinCD gradient formation.\n                  <\/jats:p>","DOI":"10.7554\/elife.101520","type":"journal-article","created":{"date-parts":[[2024,9,11]],"date-time":"2024-09-11T11:27:57Z","timestamp":1726054077000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.101520","source":"Crossref","is-referenced-by-count":0,"title":["Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis"],"prefix":"10.7554","volume":"13","author":[{"given":"Laura C","family":"Bohorquez","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/04dkp9463","id-type":"ROR","asserted-by":"publisher"}],"name":"Swammerdam 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