A molecular model that provides a framework for interpreting the wealth of functional information obtained on the E. coli F-ATP synthase has been generated using cryo-electron microscopy.

E. coli ribosomes incapable of base-pairing with the Shine-Dalgarno sequence are still selective for annotated start sites, indicating these sites are hard-wired for initiation by other mRNA features.

Cryo-EM studies reveal that incubation with ATP produces conformational intermediates of E. coli ATP synthase, in which the ε subunit is no longer in its autoinhibitory conformation.

A pre-clinical model of E. coli pneumonia reveals attenuated dynamics of MHCII-expressing mononuclear cells in neonatal lung associated with elevated susceptibility to bacterial pneumonia.

Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

Single-cell measurements combined with a new statistical framework for discriminating between models of cell cycle regulation show that chromosome initiation controls the E. coli cell cycle via two adder mechanisms.

Physical association between sister replisomes early in the E. coli replication phase promotes rapid fork progression and inhibits fork stalling.

The overexpression of RNA chaperones, including several DEAD box RNA helicases, enhances the fitness of mutationally compromised E. coli strains.

Cryo-electron microscopy structures, combined with biochemical experiments, show how the E. coli F element-encoded TraR protein regulates transcription initiation by altering RNA polymerase conformation and conformational heterogeneity.

Interactions between a mobile resistance gene and chromosomal mutations drive the evolution of high-level antibiotic resistance.