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.
A continuum of genome relationships is discovered through comparative genomics of 627 sequenced mycobacteriophages isolated and characterized in an integrated research/education initiative.
Bacterial viruses are an unexpected ‘third party’ that imposes a strong predatory pressure on a bacterial pathogen during the natural course of infection in humans.
Cryo-electron microscopy and genetics show how Staphylococcus aureus pathogenicity island 1 hijacks the assembly pathway of a helper phage for its own propagation.
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.
A detailed model of the T7 replisome with the precise positions of the helicase and polymerase at the replication fork explains how catalysis by the two enzymes is coordinated.
Degradosome-associated nucleases PNPase and RNase J2 are required for type III CRISPR immunity against diverse nucleic acid invaders originating from plasmid and phage.
A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.
