Heat shock transcription factors (HSFs) mediate the inducible transcriptional response of genes that encode heat shock proteins and molecular chaperones. HSF4 a novel member of the HSF family that shares properties with other members of the HSF family yet appears to be functionally distinct. HSF4 lacks the carboxyl-terminal hydrophobic repeat which is shared among all vertebrate HSFs and has been suggested to be involved in the negative regulation of DNA binding activity. HSF4 represents a novel HSF that exhibits tissue-specific expression and functions to repress the expression of genes encoding heat shock proteins and molecular chaperones. HSF4 is preferentially expressed in the human heart, brain, skeletal muscle, and pancreas (1). The expression of heat shock genes is controlled at the level of transcription by members of the heat shock transcription factor family in vertebrates. HSF4 is characterized by its lack of a suppression domain that modulates formation of DNA-binding homotrimer (2)
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