Bacteria must divide to increase in number and colonize their niche. Binary fission is the
most widespread means of bacterial cell division, but even this relatively simple mechanism …

Bacterial cell division is orchestrated by a tubulin homologue, FtsZ, which polymerizes to
form a ring-like structure that is both a scaffold for the assembly of the bacterial cytokinetic …

The monofunctional penicillin-binding dd-peptidases and penicillin-hydrolyzing serine β-
lactamases diverged from a common ancestor by the acquisition of structural changes in the …

FtsZ is a soluble, tubulin-like GTPase that forms a membrane-associated ring at the division
site of bacterial cells. While this ring is thought to drive cell constriction, it is not well …

Work on two diverse rod-shaped bacteria, Escherichia coli and Bacillus subtilis, has defined
a set of about 10 conserved proteins that are important for cell division in a wide range of …

The cytokinetic Z ring is required for bacterial cell division. It consists of polymers of FtsZ, the
bacterial ancestor of eukaryotic tubulin, linked to the cytoplasmic membrane. Formation of a …

ZipA and FtsA are essential division proteins in Escherichia coli that are recruited to the
division site by interaction with FtsZ. Utilizing a newly isolated temperature‐sensitive …

In the current model for bacterial cell division, FtsZ protein forms a ring that marks the
division plane, creating a cytoskeletal framework for the subsequent action of other proteins …

Bacterial cell division occurs through the formation of an FtsZ ring (Z ring) at the site of
division. The ring is composed of the tubulin-like FtsZ protein that has GTPase activity and …

The growing problem of antibiotic resistance has been exacerbated by the use of new drugs
that are merely variants of older overused antibiotics. While it is naive to expect to restrain …