Heat shock induces relocalization of epigenetic modifiers to the nucleolus, which acts as a dedicated protein quality control center that is indispensable for recovery of epigenetic regulators and epigenetic modifications.
Multiple iso-energetic-specific interactions involving the intrinsically-disordered region of sHSP HSPB1 define a quasi-ordered state, providing insights into inherited disease-associated mutations within the region that are thought to be disordered.
A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.
Small decreases in pH associated with cellular stress conditions unleash a cryptic mode of client binding in a ubiquitously expressed human small heat shock protein that is more effective at delaying client aggregation.
Ribosome assembly is monitored to promote proteostatis through a system whereby unassembled ribosomal proteins lead to activation of heat shock factor 1 and inactivation of the RP gene activator Ifh1.
Prokaryotes use polycistronic messages for coordinated translation, whereas eukaryotic cells may achieve tunable protein synthesis by packaging monocistronic mRNAs into functional multiplexes via co-transcriptional interallelic coupling and non-canonical histone-H4 functions.
Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.
The McsB kinase is critical for protein quality control in Gram-positive bacteria, assembling a gated phosphorylation chamber during heat-shock conditions to selectively mark misfolded proteins for degradation.
Quantitative dissection of the roles of chaperone binding and phosphorylation in regulating heat shock factor 1 leads to a predictive model of the dynamics of the yeast heat shock response.
