Insight into the molecular assembly of a protein with a central role in infections paves the way to understanding how Rift Valley fever virus causes disease.

Cryo-electron microscopy has been used to provide a structural interpretation of the complete action cycle of release factor 3 during translation termination, which includes a coordinated sequence of interactions with a class-I release factor and the ribosome.

Analyzing single molecules reveals that Pif1 family helicases periodically patrol DNA, which may explain this enzyme's ability to suppress genome instability at G-quadruplex motifs and transcriptional RNA-DNA hybrids (R-loops).

To regulate DNA copy number during development in Drosophila, the SUUR protein recruits Rif1 to replisomes where Rif1 inhibits replication fork progression, thus controlling copy number independently of origin firing.

The N-terminal domain (NTD) of the initiation factor eIF5 bound to the 40S subunit at the precise location vacated by eIF1 promotes tRNAi accommodation at AUG codons.

Telomere length is linked to DNA replication, and we found excessive telomeric origin firing caused by several distinct mutants did not lengthen telomeres, narrowing possible mechanisms.

The RIF1-long and short splice variants show distinct ability to protect cells from replication stress by promoting 53BP1 nuclear bodies, representing the first described functional difference between the two variants.

Bacteria produce a syringe-like structure, loaded with a single protein within the lumen of its needle-like tube, that is sufficient for stimulating animal metamorphosis.

A sharp transition in the fate of DNA ends with telomere sequences is identified, which suggests a boundary between DNA double-strand breaks and telomeres.

An interaction between the ion channel ASIC1a and the protein RIP1 is responsible for neuronal death caused by tissue acidosis.