Miguel Ángel Robles-Ramos

TL;DR: It is demonstrated that FtsZ can form crowding‐induced condensates, reminiscent of those observed for eukaryotic proteins, suggesting that phase separation may also play a functional role in the spatiotemporal organization of essential bacterial processes.

TL;DR: It is shown that, during cell division, just before splitting the daughter cells, MatP seems to localize close to the cytoplasmic membrane, suggesting that this protein might interact with lipids, which could be relevant for the coordination of the two fundamental processes in which this protein participates, nucleoid segregation and cell division.

TL;DR: The authors showed that FtsZ alone, under physiologically relevant conditions, can demix into condensates in bulk and when encapsulated in synthetic cell-like systems generated by microfluidics.

TL;DR: The ability of SlmA to bind lipids uncovered in this work extends the interaction network of this multivalent regulator beyond its well-known protein and nucleic acid recognition, which may have implications in the overall spatiotemporal control of division ring assembly.

TL;DR: Investigation of MatP interaction with lipids in vitro found that MatP, when encapsulated inside microdroplets generated by microfluidics and giant vesicles, accumulates at phospholipid bilayers and monolayers matching the lipid composition in the E. coli inner membrane.