Simultaneously inhibiting undecaprenyl phosphate production and peptidoglycan synthases promotes rapid lysis in Escherichia coli.

Peptidoglycan (PG) is a highly cross-linked polysaccharide that encases bacteria, resists the effects of turgor and confers cell shape. PG precursors are translocated across the cytoplasmic membrane by the lipid carrier undecaprenyl phosphate (Und-P) where they are incorporated into the PG superstructure. Previously, we found that one of our Escherichia coli laboratory strains (CS109) harbors a missense mutation in uppS, which encodes an enzymatically defective Und-P(P) synthase.

Endopeptidase penicillin-binding proteins 4 and 7 play auxiliary roles in determining uniform morphology of Escherichia coli.

The low-molecular-weight (LMW) penicillin-binding protein, PBP 5, plays a dominant role in determining the uniform cell shape of Escherichia coli. However, the physiological functions of six other LMW PBPs are unknown, even though the existence and enzymatic activities of four of these were established three decades ago. By applying fluorescence-activated cell sorting (FACS) to quantify the cellular dimensions of multiple PBP mutants, we found that the endopeptidases PBP 4 and PBP 7 also influence cell shape in concert with PBP 5.

beta-Lactam induction of colanic acid gene expression in Escherichia coli.

An unexpected observation led us to examine the relationship between beta-lactam exposure and synthesis of colonic acid capsular polysaccharide in Escherichia coli. Strains containing a cps-lacZ transcriptional fusion were challenged with antibiotics having various modes of action, and gene expression was detected by a disk-diffusion assay and in broth cultures. The cps genes were induced by a subset of beta-lactams but not by agents inhibiting protein synthesis or DNA replication, indicating that cps expression was specific and not due to stresses accompanying cell death or by a general inhibition of peptidoglycan synthesis.