A temperate bacteriophage reprograms the oxygen response of a bacterial signaling system by replacing a host-encoded promoter with a phage-encoded promoter.
Analysis of the Escherichia coli DnaB helicase•bacteriophage λ helicase loader (λP) complex provides insights into helicase opening, delivery to the origin and ssDNA entry, and closing in preparation for translocation.
The structure of a multi-protein DNA recombination reaction intermediate reveals how regulation is achieved by protein-mediated DNA wrapping around a core enzyme-substrate complex.
The structure of phage L's Dec demonstrates a new fold within this family of proteins, and shows modulation of capsid binding occurs through two sites, with site 1 being preferred.
Building on previous work (Wilkinson et al, 2016), it is shown that inhibition of RecBCD-induced DNA break repair can be used as a co-antibacterial strategy with quinolones.
Cryo-electron microscopy and genetics show how Staphylococcus aureus pathogenicity island 1 hijacks the assembly pathway of a helper phage for its own propagation.
