Membrane binding controls the ATPase cycle and localization of MinD in Bacillus subtilis
Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp, Petra Anne Levin, Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp · 2026
Read Membrane binding controls the ATPase cycle and localization of MinD in Bacillus subtilis by Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp, Petra Anne Levin, Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp (2026) in the Tower of Babel, a free online library of public-domain works preserved in clean, searchable text. No sign-up. The full text is served as a plain-text file at a predictable URL, where text is present: https://antarctic-labs.com/tower-of-babel/pmc-13246001.txt.
Description
Feddersen, Dyckmans, and Bramkamp dissected how a bacterial protein knows where a cell should split, in this 2026 eLife study. The Min system marks the future division site in bacteria. In Bacillus subtilis it works without the activator protein its E. coli cousin needs, raising the question of what switches its MinD motor on. Combining test-tube biochemistry with single-molecule imaging inside living cells, the team watched MinD meet the cell membrane.
Membrane binding itself activated MinD's energy-burning cycle, and ATP binding was required for the protein to let go again. Both single and paired forms of MinD could bind, but only the normal protein gathered at poles and division sites, helped by a partner protein. Locked variants spread uselessly along the membrane. The work rewrites how this division compass is regulated.
Catalog record
| CREATOR | Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp, Petra Anne Levin, Helge Feddersen, Charlotte Dyckmans, Marc Bramkamp |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 124 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |