Crosslinking the AAA+ protease interface does not abolish protein degradation by ClpAP, establishing that rotation of the AAA+ unfoldase with respect to its partner peptidase is not essential for activity.
Cryo-EM structures of the AAA+ ClpXP protease bound to an ssrA degron reveal the mechanism of substrate recognition and show how the machine transitions from recognition to translocation and unfolding.
Cryo-EM structures of the ClpXP protease reveal how protein substrates are bound, show how spiral ClpX hexamers bind symmetry-mismatched heptameric ClpP rings, and suggest mechanisms for processive substrate translocation.
A high-throughput functional genomics approach combining inducible CRISPR-interference and quantitative imaging yields an atlas of 'phenoprints' to guide gene function assignments, identify metabolic pathway-specific morphotypes, and inform antibiotic mechanism-of-action studies.
Structural and biochemical studies indicate that AAA+ ATPase employ a general mechanism to translocate a variety of substrates, including extended polypeptides, hairpins, crosslinked chains, and chains conjugated to other molecules.
High resolution structures of the essential human AAA+ ATPase TorsinA and its disease mutant in complex with an activator reveal details of the interaction that will guide drug design and further functional characterization.
A comprehensive analysis of the human MICOS complex has identified a novel subunit called QIL1 that is required for cristae junction formation in human cells and Drosophila, through its role in the assembly of the MICOS complex.