Mechanisms that enable wild mice to survive infection with strains of the Toxoplasma gondii parasite virulent enough to kill laboratory mice offer an explanation for how these parasites have been able to persist in the mouse population.
Fluorescent derivatives of a bacteriophage protein that binds double-stranded ends can trap and label genome-destabilizing double-strand DNA breaks in bacterial and human cells, and illuminate the origins of spontaneous DNA breakage in both.
The structure of the recombination complex responsible for flagellar antigen switching in Salmonella enterica, and the mechanism that regulates the site-specific DNA inversion reaction, have been determined.
While intact mir-17-92 acts as a potent oncogene in a mouse model of Burkitt’s lymphoma, one of the six mir-17-92 components antagonizes its oncogenic cooperation with c-Myc by promoting c-Myc-induced apoptosis.
High-resolution optical microscopy is used to reveal the organization of extracellular matrix proteins within the basement membrane of the blood filtration barrier in the kidney at the nanometer scale.
Evidence that C. elegans and mammals use homologous versions of the same protein (RIG-1) to activate antiviral defense mechanisms suggests that RIG-1 may have a conserved role in coupling virus recognition to virus destruction.