A novel component of type III protein secretion systems involved in the assembly of the secretion machine is reported.

In budding yeast cells, slow monomeric septin GTPase activity and the cytosolic GTP:GDP ratio dictate the relative incorporation of alternative subunits during septin hetero-oligomer assembly, which proceeds by discrete, ordered steps dependent on allostery between interaction interfaces.

Higher-order assembly enables and links pathogen recognition and downstream steps in the TRIM5-mediated anti-HIV response.

Folding and unfolding of a 6-helix bundle controls HIV assembly and maturation.

PI(4,5)P2 plays a much broader role during the HIV-1 particle assembly process than assumed; it is indispensable not only for recruitment of Gag to the plasma membrane but also for the maintenance of Gag assemblies.

The CAF1 complex binds single histone H3-H4 dimers, and two such complexes associate with extended DNA elements to ensure the deposition of H3-H4 tetramers, the first step in the assembly of nucleosomes.

The Chd1 motor protein performs two functionally distinct ATP-dependent activities, nucleosome assembly and chromatin remodeling, to generate periodic arrays of nucleosomes.

The packaging signal in HIV-1 genomic RNA supports in vitro particle assembly more efficiently than control RNAs, probably explaining its selective packaging during virus assembly in vivo.

The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.

Comprehensive structural and compositional characterization of the in vivo 30S ribosomal assembly landscape reveals parallel pathways for 3′-domain formation and a previously unknown role for the assembly factor RimP.