Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis
Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen, Petra Anne Levin, Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen · 2026
Read Membrane affinity difference between MinD monomer and dimer is not crucial for MinD gradient formation in Bacillus subtilis by Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen, Petra Anne Levin, Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen (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-13537761.txt.
Description
Laura Bohorquez and five co-authors test whether the grip gap between single and paired forms of the MinD protein is key to its gradient in Bacillus subtilis, a rod shaped bacterium. The Min system stops division at cell poles, which avoids tiny cells. The study came out in twenty twenty-six.
In a cousin germ, MinD swings pole to pole with a partner protein. This species lacks that partner and holds a still gradient with a membrane anchor at poles and division sites. The team finds both forms of MinD grip the membrane about alike here. MinD meets its anchor as a pair, which reshapes how the gradient model should be built.
Catalog record
| CREATOR | Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen, Petra Anne Levin, Laura C Bohorquez, Henrik Strahl, Davide Marenduzzo, Martin J Thiele, Frank Burmann, Leendert Hamoen |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 82 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |