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.
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.
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.