Heat shock factor (HSF) is a transcriptional activator of heat shock genes: it binds specifically to heat shock promoter elements, which arepalindromic sequences rich with repetitive purine and pyrimidine motifs.Under normal conditions, HSF is a homo-trimeric cytoplasmic protein, butheat shock activation results in relocalisation to the nucleus.Each HSF monomer contains one C-terminal and three N-terminal leucine zipperrepeats. Point mutations in these regions result in disruption ofcellular localisation, rendering the protein constitutively nuclear.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. The DNA-binding componentof HSF lies to the N terminus of the first NLS region, and is referred toas the HSF domain.