Heat shock factor 1 is involved in estrogen-induced chromatin remodeling in estrogen receptor-positive breast cancer cells.

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.

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.

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.

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

Helitron transposable elements, by providing high density transcription factor binding sites upstream of host genes, have diversified the heat shock response within and among Caenorhabditis species.

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.

Dynamic regulation of the heat shock response depends on a negative feedback loop in which Hsf1 activates expression of Hsp70 and Hsp70 specifically and directly represses Hsf1 transactivation.

Heat-induced local unfolding allows Hsf1 to form trimers and bind to DNA, which depends on Hsf1 concentration and is promoted, not inhibited, by Hsp90.