Heat shock factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1

A1 Journal article (refereed)


Internal Authors/Editors


Publication Details

List of Authors: Östling P, Björk JK, Roos-Mattjus P, Mezger V, Sistonen L
Publication year: 2007
Journal: Journal of Biological Chemistry
Journal acronym: J BIOL CHEM
Volume number: 282
Issue number: 10
Start page: 7077
End page: 7086
Number of pages: 10
ISSN: 0021-9258
eISSN: 1083-351X


Abstract

The heat shock response is a defense reaction activated by proteotoxic damage induced by physiological or environmental stress. Cells respond to the proteotoxic damage by elevated expression of heat shock proteins (Hsps) that function as molecular chaperones and maintain the vital homeostasis of protein folds. Heat shock factors (HSFs) are the main transcriptional regulators of the stress-induced expression of hsp genes. Mammalian HSF I was originally identified as the transcriptional regulator of the heat shock response, whereas HSF2 has not been implicated a role in the stress response. Previously, we and others have demonstrated that HSF1 and HSF2 interact through their trimerization domains, but the functional consequence of this interaction remained unclear. We have now demonstrated on chromatin that both HSF1 and HSF2 were able to bind the hsp70 promoter not only in response to heat shock but also during hemin-induced differentiation of K562 erythroleukernia cells. In both cases an intact HSF1 was required in order to reach maximal levels of promoter occupancy, suggesting that HSF1 influences the DNA binding activity of HSF2. The functional consequence of the HSFI-HSF2 interplay was demonstrated by real-time reverse transcription-PCR analyses, which showed that HSF2 was able to modulate the HSFI-mediated expression of major hsp genes. Our results reveal, contrary to the predominant model, that HSF2 indeed participates in the transcriptional regulation of the heat shock response.

Last updated on 2019-13-10 at 04:07