Heat shock factor (HSF)-type, DNA-binding
IPR000232
Definition
Heat shock factor (HSF) is a transcriptional activator of heat shock genes [[cite:PMID:2257625], [cite:PMID:19864465]]: 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.
8 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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