In vivo and in vitro approaches uncover a new function for the β-barrel OmpA and reveal how it interacts with the stress sensor lipoprotein RcsF.

Bacterial outer membrane proteins are recognized by BamD at specific signals located in multiple β-strands at the C-terminus of these proteins, and this recognition is important for efficient outer membrane protein assembly and maintaining the integrity of outer membrane.

The envelope stress factor DolP associates with the outer membrane protein assembly machinery and supports proper folding and functioning of BamA contributing to preserve envelope integrity.

Mutations that block assembly of the interlocked RcsF/β barrel protein complex prevent detection of lipopolysaccharide stress and activation of Rcs signal transduction pathway.

The protein translocation apparatus of the inner- (Sec) and outer-membrane (BAM) interact to form a trans-periplasmic super-complex capable of long-range, PMF-dependent conformational changes to facilitate efficient outer-membrane protein maturation.

An example of a deep learning-based strategy to discover novel protein-protein interactions and predict their complex structures at high accuracy.

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

Bacterial warfare protein colicin E1 opens its hinge to plug antibiotic efflux pump TolC and potentiate antibiotics.

Outer membrane vesicles serve as decoys to reduce the chance of direct polymyxin B (PMB) binding to cells, which partly explains why many clinical isolates and microbial communities can be protected against PMB treatment.

Multiple RNA-seq approaches globally mapped RNA 3´ ends resulting in the discovery of numerous and diverse RNA regulators.