A response regulator acquired via lateral gene transfer has rewired an ancestral genetic circuitry and regulates alternative pathogenic lifestyles.

Inside the acidic vacuole, expression, DNA binding and DNA binding affinity of the Salmonella regulator SsrB is stimulated by acid pH.

A single conserved residue – histidine 12 – confers pH-sensitive DNA binding to the Salmonella Typhimurium SPI-2 transcriptional regulator SsrB, thereby regulating Salmonella virulence.

Cryo-EM structures of the AAA+ ClpXP protease bound to an ssrA degron reveal the mechanism of substrate recognition and show how the machine transitions from recognition to translocation and unfolding.

The absence of oxygen prompts Staphylococcus aureus cells to rupture resulting in increased formation of biofilms, which are the etiological agents of recurrent infections.

Cells resolve unassigned codons with near-cognate suppression, frameshifting, and ribosomal rescue mechanisms, demonstrating that unassigned codons are permissible in both natural and engineered genetic codes as barriers to horizontal gene transfer.

Understanding of bacterial protein degradation is illuminated by cryo-EM structures of the substrate-bound ClpXP complex from Neisseria meningitidis at 2.3 to 3.3 Å resolution.

The AAA+ protein unfolding motor ClpX grips substrates with the uppermost part of its substrate-binding pore, and requires interactions with hydrophobic amino acid side chains to operate with optimal efficiency.

The LOVdeg tag is a versatile tool for bacterial optogenetics, offering modular, blue light-inducible protein degradation for a range of synthetic biology and metabolic engineering applications.

Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.