Genetic and molecular analyses identify and characterize an evolutionary battle over lysis timing wherein a bacteriophage delays lysis through lysis inhibition while a defensive phage satellite accelerates lysis.
The first structure of a bacteriophage-encoded S-adenosyl methionine degrading enzyme was solved and demonstrated to catalyze a unimolecular lyase reaction occurring at the domain interface of a trimeric structure.
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.
A new way to alter the genome of bacteriophages helps produce large libraries of variants, allowing these bacteria-killing viruses to be designed to target species harmful to human health.
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.
