Class-A penicillin-binding proteins are dispensable for rod-like cell-shape but essential for mechanical integrity by sensing and repairing cell-wall defects locally, as investigated in the model system Escherichia coli.

The synthesis of bacterial cell wall peptidoglycan was reconstituted in lipid bilayers and detected by a novel Förster resonance energy transfer real-time assay.

PBP-lipo is an essential cell-wall synthesis enzyme in Mycobacterium abscessus that localizes to the septum and whose expression is required for normal cell growth and division, as well as mediating sensitivity to several antibiotics including the β-lactams, ampicillin, and amoxicillin.

Environmental specialization of bacterial cell wall synthases influences intrinsic resistance to cell wall active antibiotics.

Balanced peptidoglycan synthesis requires regulators, including sigma-I and WalKR, that coordinate the diffusive action of class A PBPs and the directional motion of the MreB-directed elongasome.

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

Production of the L,D-transpeptidase YcbB and elevated synthesis of the (p)ppGpp alarmone reveals a new mode of peptidoglycan polymerization that bypasses the D,D-transpeptidase activity of PBPs and leads to broad-spectrum β-lactam resistance in Escherichia coli.

Selective removal of Wall Teichoic Acids from the envelope of Streptococcus pneumoniae prevents bacteriolysis and directs zonal cell wall synthesis.

A newly established reversible model of membrane departitioning and repartitioning in bacteria uncovers the role of a cell wall synthase in regulating membrane partitioning.

The N-terminal domain of Staphylococcus aureus GpsB, a scaffolding protein, forms an atypical asymmetric dimer and binds to the C-termini of FtsZ and PBP4, influencing the localization and regulation of both the Z-ring and cell wall synthesis.