Dynamics of the full length and mutated heat shock factor 1 in human cells.

Gaëtan Herbomel 1 Meike Kloster-Landsberg 2 Eric Folco 1 Edwige Col 1 Yves Usson 3 Claire Vourc'H 1 Antoine Delon 2 Catherine Souchier 1, *
* Auteur correspondant
1 INSERM U823, équipe 10 (Stress et Dynamique de l'Organisation du Génome)
INSERM U823 - Institut d'oncologie/développement Albert Bonniot de Grenoble
2 MOTIV
LIPhy - Laboratoire Interdisciplinaire de Physique [Saint Martin d’Hères]
3 DyCTiM
TIMC-IMAG - Techniques de l'Ingénierie Médicale et de la Complexité - Informatique, Mathématiques et Applications [Grenoble]
Abstract : Heat shock factor 1 is the key transcription factor of the heat shock response. Its function is to protect the cell against the deleterious effects of stress. Upon stress, HSF1 binds to and transcribes hsp genes and repeated satellite III (sat III) sequences present at the 9q12 locus. HSF1 binding to pericentric sat III sequences forms structures known as nuclear stress bodies (nSBs). nSBs represent a natural amplification of RNA pol II dependent transcription sites. Dynamics of HSF1 and of deletion mutants were studied in living cells using multi-confocal Fluorescence Correlation Spectroscopy (mFCS) and Fluorescence Recovery After Photobleaching (FRAP). In this paper, we show that HSF1 dynamics modifications upon heat shock result from both formation of high molecular weight complexes and increased HSF1 interactions with chromatin. These interactions involve both DNA binding with Heat Shock Element (HSE) and sat III sequences and a more transient sequence-independent binding likely corresponding to a search for more specific targets. We find that the trimerization domain is required for low affinity interactions with chromatin while the DNA binding domain is required for site-specific interactions of HSF1 with DNA.
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PLoS ONE, Public Library of Science, 2013, 8 (7), pp.e67566. 〈10.1371/journal.pone.0067566〉
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Gaëtan Herbomel, Meike Kloster-Landsberg, Eric Folco, Edwige Col, Yves Usson, et al.. Dynamics of the full length and mutated heat shock factor 1 in human cells.. PLoS ONE, Public Library of Science, 2013, 8 (7), pp.e67566. 〈10.1371/journal.pone.0067566〉. 〈inserm-00847765〉

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