Heat shock factor (HSF)-type, DNA-binding (IPR000232)

Short name: HSF_DNA-bd

Domain relationships


Heat shock factor (HSF) is a transcriptional activator of heat shock genes [PMID: 2257625]: it binds specifically to heat shock promoter elements, which are palindromic sequences rich with repetitive purine and pyrimidine motifs [PMID: 2257625]. Under normal conditions, HSF is a homo-trimeric cytoplasmic protein, but heat shock activation results in relocalisation to the nucleus [PMID: 1871105]. Each HSF monomer contains one C-terminal and three N-terminal leucine zipper repeats [PMID: 1871106]. Point mutations in these regions result in disruption of cellular localisation, rendering the protein constitutively nuclear [PMID: 1871105]. Two sequences flanking the N-terminal zippers fit the consensus of a bi- partite nuclear localisation signal (NLS). Interaction between the N- and C-terminal zippers may result in a structure that masks the NLS sequences: following activation of HSF, these may then be unmasked, resulting in relocalisation of the protein to the nucleus [PMID: 1871106]. The DNA-binding component of HSF lies to the N terminus of the first NLS region, and is referred to as the HSF domain.

GO terms

Biological Process

GO:0006355 regulation of transcription, DNA-templated

Molecular Function

GO:0043565 sequence-specific DNA binding
GO:0003700 sequence-specific DNA binding transcription factor activity

Cellular Component

GO:0005634 nucleus

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns