The prokaryotic actin homologue MreB forms antiparallel double filaments in vitro and in vivo, an architecture that is unprecedented among the actin family of proteins.

The helical bacterium Helicobacter pylori patterns cell wall synthesis using two distinct cytoskeletal proteins, CcmA and MreB, to achieve its characteristic shape.

Analyses of the stalked budding bacterium Hyphomonas neptunium and its spiral-shaped relative Rhodospirillum rubrum reveal a conserved morphogenetic module that controls the establishment of complex bacterial cell shapes.

Close evolutionary relationship between eukaryotic F-actin and crenarchaeal crenactin protein is supported by a near-atomic cryoEM structure of double helical filaments, that are inhibited by arcadin-2 through binding to crenactin's hydrophobic groove.

First 3D-structure and first observation of organized protofilaments of MreB from a Gram-positive bacterium, suggesting a model where ATP drives the formation of dynamic pairs of MreB protofilaments on a lipid surface.

For initiation of cell-wall insertion, the cross-linking enzyme PBP2 stably binds to a component of the cell envelope that is different from MreB filaments.

Mycobacteria employ plasma membrane compartments to organize their cell wall synthesis, and the finalized cell wall compartmentalizes the plasma membrane to promote an environment conducive to its own synthesis.

Correct cell wall synthesis in bacteria depends on flotillin-mediated membrane fluidity.