Canonical centriole duplication is much less prone to errors than de novo synthesis of centrioles, but neither depends on self-oligomerization of the centriole protein SAS-6.
A simple, yet elegant method for robust self-assembly of diverse membrane proteins into soluble peptide nanoparticles for their structural and functional analysis in detergent-free solutions.
The scanning-assisted clustering mechanism of IFI16 not only allows efficient assembly on exposed foreign-dsDNA, but also suppresses the engagement of chromatinized self-dsDNA.
In the cytosol, the proteins constituting cell-matrix adhesion sites form multi-protein building blocks which enter and leave these sites unaltered, thereby contributing to their rapid and correct self-assembly.
New insights into the assembly and membrane interactions of the caveolar coat complex reveal the reversible association/dissociation of distinct subcomplexes onto the membrane, which differs from the assembly/disassembly of clathrin-coated pits.
The length-dependent growth rate of bacterial flagellar filament is determined by the flagellin loading speed, loading strength and its diffusion process.
Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.
A structural and biochemical study of human SYCP3 provides the first molecular model for the three-dimensional organisation that is imposed upon chromosomal DNA during meiosis and is essential for genetic exchange and fertility.
Molecular simulations show how hydrophobicity and conformational disorder underlie the phase separation of elastin-like peptides and the elasticity of human tissues.
How nuclear pore complexes establish their permeability barrier has been a long-standing question; now, this process can be reconstituted by a surprisingly simple and rapid self-assembly of Nup98 FG domains into selective FG phases.
