Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1

Thomson, S; Hollis, A; Hazzalin, CA; Mahadevan, LC

HERO ID

1354244

Reference Type

Journal Article

Year

2004

Language

English

PMID

15327774

HERO ID 1354244
In Press No
Year 2004
Title Distinct stimulus-specific histone modifications at Hsp70 chromatin targeted by the transcription factor heat shock factor-1
Authors Thomson, S; Hollis, A; Hazzalin, CA; Mahadevan, LC
Journal Molecular Cell
Volume 15
Issue 4
Page Numbers 585-594
Abstract A question of major current interest is whether histone modification at a given gene correlates simply with transcriptional status or if distinctive modifications appear depending on how that gene is activated. The stress-inducible gene Hsp70 is activated by heat shock or by sodium arsenite. Heat shock produces acetylation of histone H4 at Hsp70 chromatin, whereas arsenite produces both H4 acetylation and H3 phosphorylation at the gene. Histone H3 remains markedly hypoacetylated at Hsp70 under these conditions. Arsenite, but not heat shock, requires signaling via p38 MAP kinase for Hsp70 induction and histone H3 phosphorylation. However, independently of p38 MAP kinase, both stresses strongly activate the transcription factor Hsf1. Using Hsf1-/- cells, we show that this factor is responsible for targeting histone H4 acetylation to Hsp70 chromatin. We establish here that histone modifications at inducible genes are not simply a reflection of transcriptional activity, but are strictly dependent on the stimulus used for induction.
Doi 10.1016/j.molcel.2004.08.002
Pmid 15327774
Wosid WOS:000223565200012
Is Certified Translation No
Dupe Override No
Comments Source: Web of Science WOS:000223565200012
Is Public Yes
Language Text English