What is HSF protein?
Trimerization of heat shock transcription factor (HSF) The HSF is a sequence-specific DNA binding protein that binds specifically to HSE with high affinity. The activation of HSF and its subsequent binding to HSE are key steps in regulating the expression of almost all heat shock genes.
What is HSF activated by?
HSF preexists mostly as an inert state in unstressed cells and is converted quickly to an active state to induce the heat shock genes including HSP genes during heat shock. HSF is also activated at different levels by a variety of environmental and pathophysiological stresses.
What does HSF bind?
Description. Heat shock factor (HSF) is a transcriptional activator of heat shock genes. : it binds specifically to heat shock promoter elements, which are palindromic sequences rich with repetitive purine and pyrimidine motifs. .
What is HSF biology?
In molecular biology, heat shock factors (HSF), are the transcription factors that regulate the expression of the heat shock proteins.
What is the function of HSF1?
Heat shock factor 1 (HSF-1) is the major regulator of heat shock protein transcription in eukaryotes. In the absence of cellular stress, HSF-1 is inhibited by association with heat shock proteins and is therefore not active.
What is the HSF domain?
The DNA-binding component of HSF lies to the N-terminus of the first NLS region, and is referred to as the HSF domain. Humans express the following heat shock factors:
Is HSF1 a potential target for the treatment of protein aggregation?
Given its function has been extensively studied in recent years, HSF1 is considered a potential target for the treatment of disorders associated with protein aggregation.
How do stress-denatured proteins compete with HSF1 for transcriptional activity?
In heat shocked cells, stress-denatured proteins compete with HSF1 homotrimeric DNA-bound form for association of the HSP90-dependent multichaperone complex, and hence alleviating repression of HSF1-mediated transcriptional activity (PubMed: 11583998 ).