D. Kureisaite-Ciziene

This study identifies PRC domain proteins as essential components of the FtsZ-based cell division machinery in archaea, showing they form complexes with SepF and FtsZ and are required for proper cell division.

This study shows that FtsA forms curved antiparallel double filaments when bound to FtsN, similar to MreB, and suggests these structures orient septal PG synthesis during bacterial division.

This study reveals that bactofilins form non-polar filaments that bind directly to membranes, with conserved N-terminal tails mediating membrane interaction.

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

This study identifies a conformational switch in FtsZ that enables treadmilling and cooperative filament assembly during bacterial cell division.