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Mol. Cell. Biol., Jan 1997, 469-481, Vol 17, No. 1
A Nakai, M Tanabe, Y Kawazoe, J Inazawa, RI Morimoto and K Nagata
Heat shock transcription factors (HSFs) mediate the inducible
transcriptional response of genes that encode heat shock proteins and
molecular chaperones. In vertebrates, three related HSF genes (HSF1 to - 3)
and the respective gene products (HSFs) have been characterized. We report
the cloning and characterization of human HSF4 (hHSF4), a novel member of
the hHSF family that shares properties with other members of the HSF family
yet appears to be functionally distinct. hHSF4 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. hHSF4 is preferentially expressed in the human heart, brain,
skeletal muscle, and pancreas. Transient transfection of hHSF4 in HeLa
cells, which do not express hHSF4, results in a constitutively active DNA
binding trimer which, unlike other members of the HSF family, lacks the
properties of a transcriptional activator. Constitutive overexpression of
hHSF4 in HeLa cells results in reduced expression of the endogenous hsp70,
hsp90, and hsp27 genes. hHSF4 represents a novel hHSF that exhibits tissue-
specific expression and functions to repress the expression of genes
encoding heat shock proteins and molecular chaperones.
Copyright © 1997, American Society for Microbiology
HSF4, a new member of the human heat shock factor family which lacks properties of a transcriptional activator
Department of Cell Biology, Kyoto University, Japan. nakai@chest.kyoto- u.ac.jp
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