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Fig. 1. The regulatory model of transcriptional activation leading to the de novo synthesis of heat-shock proteins (hsps). Under non-stressful conditions, heat-shock factor-1 (HSF1) monomers are associated with a chaperone complex that consists at least of hsp70, hsp90 and hsp40 (for references, see text). During thermal stress, the chaperones dissociate from the complex and bind to unfolded proteins. Dissociation of the complex thus frees HSF1 monomers, which are then able to move into the nucleus and bind to the heat-shock element (HSE). HSF1 trimers bound to the HSE become hyper-phosphorylated (P) before they are transcriptionally competent. As hsp levels increase, their binding to HSF1 triggers its dissociation from the HSE, leading to a decrease in hsp gene transcription (diamond-shaped ends indicate this inhibitory effect).
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