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.
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.
RIG-I Singleton-Merten syndrome mutations either mimic or freeze the protein in an ATP-bound state and lead to autoimmune signalling through a gain-of-function recognition of self-RNA.
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.
A cryo-electron microscopy structure of a substrate-bound Vps4-Vta1 AAA ATPase reveals an asymmetric hexameric ring and suggests how nucleotide-induced changes in subunit interfaces translocate polypeptides into the central pore.
