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Vol. 20, Issue 23, 4976-4984, December 1, 2009
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*Institut National de la Santé et de la Recherche Médicale, U823, Institut Albert Bonniot, Université Joseph Fourier, F-38706 Grenoble, France;
IEO Experimental Oncology, IFOM-IEO Campus, I-20139 Milan, Italy; and
Centre de Biologie du Developpement, IFR 109; CNRS; UPS, Université Toulouse 3; UMR 5547, F-31062 Toulouse Cedex 09, France
Submitted April 24, 2009;
Revised September 9, 2009;
Accepted September 23, 2009
Monitoring Editor: A. Gregory Matera
A major regulatory function has been evidenced here for HSF1, the key transcription factor of the heat-shock response, in a large-scale remodeling of the cell epigenome. Indeed, upon heat shock, HSF1, in addition to its well-known transactivating activities, mediates a genome-wide and massive histone deacetylation. Investigating the underlying mechanisms, we show that HSF1 specifically associates with and uses HDAC1 and HDAC2 to trigger this heat-shock–dependent histone deacetylation. This work therefore identifies HSF1 as a master regulator of global chromatin acetylation and reveals a cross-talk between HSF1 and histone deacetylases in the general control of genome organization in response to heat shock.
Address correspondence to: (Claire.vourch{at}ujf-grenoble.fr).
Abbreviations used: HAT, histone acetyl transferase; HDAC, histone deacetylase; HSF1, heat-shock factor 1; HSP, heat-shock protein.