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.
Blastoderm tissue organization and patterning in zebrafish explants is driven by a genetically encoded and controlled self-assembly mechanism, rather than a bonafide self-organization mechanism.
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.
Rudimentary cross-catalytic replication can be established by double-hairpins of tRNA-like sequences, implying that replication and translation could have emerged along a common evolutionary trajectory.
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.
Nanoscaleimaging reveals that animal septins form dense filamentous networks on biomimeticlipid membranes, explaining how septins may regulate cell surface rigidity.
Nucleation, elasticity theory, and simulations were combined to construct a general phase diagram that elucidates the conditions for successful viral assembly and the key factors to prevent it.
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.
