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Empirical energy landscape allows simulating the structural dynamics of the proteasomal ATPase complex, which yields predictions that are widely consistent with experimental observations and reveals the functional mechanism of the proteasome in substrate degradation.

Bacterial Type IV restriction-modification systems display remarkable, previously unnoticed diversity of complex gene and domain architectures, and are predicted to couple antiphage immunity with the abortive infection form of defense.

Deep mutagenesis of a clamp-loader complex reveals a critical hydrogen-bonded junction that is important for allosteric communication in oligomeric AAA+ ATPases.

A phage-encoded protein inhibits a bacterial replicative helicase loading factor by exploiting an internal site that auto-regulates loader self-assembly and ATPase activity.

Prokaryotic TRADD-N and Death-like adaptor domains in diverse predicted apoptosis and immune systems from multicellular prokaryotes and metazoans indicate the common origin of key apoptosis mechanisms required for the stabilization of multicellularity.

The GTPase Nog1 orchestrates stalk assembly, peptidyl transferase centre maturation and polypeptide exit tunnel quality control.

The structure of a substrate-engaged AAA+ unfoldase suggests a model for processive unfolding that is supported by biochemical data.

The 26S proteasome lid subcomplex acts as an external scaffold whose interactions with the ATPase motor stabilize the substrate-engagement-competent state, and control conformational changes upon engagement for subsequent degradation steps.

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.

Head-to-head interactions of regulatory coiled-coil domains control activity of the central bacterial AAA+ protein ClpC by promoting formation of a reversible resting state.