Probing the DNA motor SpoIIIE at the single-molecule level has revealed its force-generating step, rich translocation dynamics during motor operation and a novel, bi-phasic mechanical response to opposing force.

The subunits of the SpoIIIE motor contact the 5'→3' strand of DNA in sequence to rapidly translocate the DNA across a membrane.

Mutations within the ATPase domain of RIG-I in patients with Singleton-Merten Syndrome prevent ATP-hydrolysis dependent dissociation of RIG-I from double-stranded RNA and lead to unintentional constitutive signaling through increased binding of endogenous RNA.

The Mcm2-7 motor unwinds DNA using an approach distinct from that of superfamily III helicases, and accesses multiple ring configurations and assembly states during the initiation of DNA replication.

LAP1 adopts an AAA+ like fold that, while unable to bind nucleotide, can enhance ATPase activity in the neighboring TorsinA protomer in an unusual heterohexameric ring, via an arginine finger.

Cryo-EM reveals the regulation of RUVBL1 and RUVBL2 AAA-ATPases by DHX34, a helicase involved in nonsense-mediated mRNA decay (NMD), and suggests mechanisms for how RUVBL1 and RUVBL2 function in NMD.

Protein disaggregases employ two mechanically-linked ATPase rings that are under steric control by a wrapped-around coiled-coil belt.

Genetic labeling of cells that survive executioner caspase activity in Drosophila reveals distinct patterns in different tissues.

A single-cell atlas of the developing Drosophila wing disc at two time points enables a detailed understanding of the signals exchanged between different cell populations during development.

Structure-guided biochemistry defines how the coupling between nucleic acid substrate binding and ATPase activity is used by a molecular switch to load ring-shaped motor proteins onto single-stranded DNA.