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.

Hsp70 restricts DNA binding activity of Hsf1 to control the width and amplitude of the heat-shock regulon.

A new unfolded protein response has been discovered that is distinct from the heat shock response and protects mammalian cells from proteotoxic stress.

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.

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.

Phylogenetic and biochemical analysis reveals crucial role of two substitutions in the α–crystallin domain for development of new functionality of IbpA chaperone after the loss of paralogous IbpB in Erwiniaceae.

The chaperones Hsp70 and Sis1 collaborate to repress the heat shock response and are both transcriptional targets of the heat shock response, yet only Hsp70 acts as a negative feedback regulator of the heat shock response.

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.

When translation stops, cells require intracellular acidification to turn on the conserved heat shock response during stress, and stress-triggered acidification (common in eukaryotes) is adaptive, promoting cell and population fitness.

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.