Claudine Fraipont

TL;DR: A two‐step model for bacterial division is suggested in which the Z‐ring is involved in the switch from cylindrical to polar peptidoglycan synthesis, whereas the much later localizing cell division proteins are responsible for the modification of the envelope shape into that of two new poles.

TL;DR: Significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.

TL;DR: These studies have demonstrated, for the first time, a direct interaction between a class B PBP (PBP3) and a class A PBP(PBP1B) in vitro and in vivo, indicating that different murein synthases might act in concert to enlarge the muresin sacculus during cell division.

TL;DR: FtsN could have a role in controlling or modulating the activity of PBP1B during cell division in Escherichia coli.

TL;DR: In vitro peptidoglycan synthesis assays provide novel insights into the cooperativity of peptidglycan synthases with different activities, and provide a possible explanation for the depletion of lipid II precursors in penicillin‐treated cells.