A remarkable case of the common evolutionary origin of a prominent spider venom component.

Salmonella antibacterial effectors act on Y-shaped DNA substrates resembling replication forks or transcription bubbles and lead to DNA double-strand breaks.

Distinct surfaces of an interbacterial competition cell wall toxin mediate interactions with different cellular binding partners, resulting in an inherent evolutionary trade-off across the toxin superfamily.

Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.

Genomics and genetics were used to identify specialized metabolites employed by Pseudomonas bacteria to suppress the growth of potato pathogens, which revealed a key role for cyclic lipopeptides.

The sensory regulatory system of the cholera causative involves the detection of bile acids by direct interaction with the inner membrane protein complex formed by ToxR and ToxS, thereby inducing concentration-dependent structural changes.

A statistical approach for predicting non-active site residues responsible for allostery, cooperativity, or other subtle but functionally important interactions is described and applied to various protein families.

Interbacterial interactions can promote mutagenesis, and possibly adaptation, when intoxicated cells survive exposure to type VI secretion-delivered DNA deaminase toxins.

The upper airway commensal, Neisseria cinerea, competes with related species using a T6SS, with antagonism modulated by the spatial dynamics of attacker and prey strains growing in a mixed community.

Structural analysis of the HipBST toxin–antitoxin system from E. coli shows how a toxin kinase has been split into two proteins and encodes its own inhibitor.