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.

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.

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.

A pooled genetic screening method measures the effect of knocking down every gene on a transcriptional stress response to proteotoxic stress (the heat shock response) using only nucleic acid sequencing, without cell enrichment or single-cell isolation.

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.

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.

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

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.

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

In starving yeast exposed to thermal stress, a transient drop in intracellular pH helps to trigger the heat shock response.