T. den Blaauwen

This study shows that activating the Rcs phosphorelay in E. coli reduces growth rate and alters FtsZ distribution, with effects mediated through growth-rate changes rather than direct regulation.

This study characterizes YhcB, a conserved gamma-proteobacterial protein, showing it is essential for cell division and envelope integrity through genetic, structural, and interaction analyses.

This paper shows that PBP4 localizes at midcell during septal PG synthesis in E. coli and is important for the timing of divisome assembly.

The paper investigates how MreC and MreD regulate the interaction between PBP2 and RodA in the elongasome, showing that MreC modulates this interaction while MreD suppresses it, suggesting a mechanism for controlling elongasome activity.

This study shows that ZapA tetramerization is necessary for proper localization and interaction with ZapB in E. coli, affecting cell division and chromosome segregation.

This study identifies NlpI as a scaffold for PG hydrolases in E. coli, forming multi-enzyme complexes that coordinate PG synthesis and hydrolase activity.

The paper shows MatP interacts with lipid membranes in E. coli during cell division, suggesting lipid binding modulates its localization and function without requiring DNA.

This study shows MurJ is recruited to midcell during E. coli cell division and depends on lipid II synthesis and divisome activity.

The paper develops a new fluorescent protein variant, sfTq2ox, optimized for the bacterial periplasm to enable efficient FRET for studying cell division antibiotic targets.

This study investigates the interaction between FtsQ and FtsB in E. coli, revealing key residues and structural details critical for cell division.