The pilus extrusion/DNA uptake system of Thermus thermophilus contains a 13-mer of the 757-residue PilQ protein and a tightly bound protein outside the outer membrane with a role in DNA binding.

The model organism Tetrahymena thermopile carries two nuclei with distinct genomes: an unrearranged germline genome with five chromosomes, and a somatic genome reduced in size by a third and with 181 chromosomes.

Electron cryo-tomography reveals a huge conformational change in the secretin domain of the type IV pilus machinery that occurs when the channel opens for pilus extrusion.

eMags is an engineered photodimerizer pair for optogenetic modulation in mammalian cells that is especially suited for the manipulation of intracellular processes occurring in small volumes or subcellular organelles.

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

The structural and functional analysis of the ATP-dependent RNA helicase Prp43 provides insights into the mechanisms of RNA binding and translocation, which could serve as paradigm for all DEAH-box proteins.

The genome of Thermovibrio ammonificans encodes ancestral pathways (e.g., hydrogen oxidation) and more recently acquired ones (e.g., nitrate reduction) and a hybrid pathway for CO₂ fixation.

Cryo-EM structures of rotary V-ATPase reveal the ON-OFF switching mechanism of H⁺ translocation in the V_o membrane domain.

Interconnected RNA processing mechanisms ensure the fidelity of non-conventional mRNA splicing during the unfolded protein response.

Components of the nuclear pore complex share structural and functional features with soluble nuclear transport receptors, which suggests that there may be an evolutionary relationship between these two types of protein.