Multi-site FRET measurements of moPrP oligomerization at low pH indicate that major conformational changes take place as monomers reversibly transform into large oligomers, which subsequently disassemble reversibly into small oligomers.
The bacterium Escherichia coli possesses a permissive cytoplasmic environment and the requisite molecular machinery to support the propagation of prions.
Overcoming image-processing problems in the analysis of the ClpB chaperone provides a new structural model and regulatory mechanism, based on clear density for the coiled-coil domain and supported by various biochemical data.
Courtney L Klaips, Megan L Hochstrasser ... Tricia R Serio
Cell division imposes a limit on proteostasis capacity by reducing chaperone accumulation, but chaperone-substrate interactions reverse these events to allow clearance of even chronically misfolded protein amyloids.
The cisternae of the Golgi contain two functionally distinct domains: the central areas, which remain stationary, and the edges or rims, which are mobile.
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.
Blake W Tye, Nicoletta Commins ... L Stirling Churchman
Rapidly proliferating cells are at risk of compromised cell fitness due to proteostasis collapse from perturbations that interfere with ribosome biogenesis.
A combination of transcriptomics, proteomics and modelling identifies a network of interacting protein phosphatases that act as a biological switch to move cells from the stem cell compartment to the differentiated compartment in cultured human epidermis.
Michael H Hayes, Elizabeth H Peuchen ... Daniel L Weeks
The equilibrium between solubility and aggregation of proteins in the nucleus is controlled by co-aggregates like RNA and the action of ATP as both an energy source and a destabilizing chemical agent.
