|SMART accession number:||SM00415
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|Interpro abstract (IPR000232):
||Heat shock factor (HSF) is a transcriptional activator of heat shock genes [(PUBMED:2257625)]: it binds specifically to heat shock promoter elements, which are palindromic sequences rich with repetitive purine and pyrimidine motifs [(PUBMED:2257625)]. Under normal conditions, HSF is a homo-trimeric cytoplasmic protein, but heat shock activation results in relocalisation to the nucleus [(PUBMED:1871105)]. Each HSF monomer contains one C-terminal and three N-terminal leucine zipper repeats [(PUBMED:1871106)]. Point mutations in these regions result in disruption of cellular localisation, rendering the protein constitutively nuclear [(PUBMED: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 [(PUBMED: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 process:||regulation of transcription, DNA-templated (GO:0006355)|
|GO component:||nucleus (GO:0005634)|
|GO function:||sequence-specific DNA binding (GO:0043565), sequence-specific DNA binding transcription factor activity (GO:0003700)|
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