Gcn5- and Elp3-induced histone H3 acetylation regulates hsp70 gene transcription in yeast.

Abstract	The purpose of this study was to elucidate the mechanisms by which histone acetylation participates in transcriptional regulation of hsp70 (heat-shock protein 70) genes SSA3 and SSA4 in yeast. Our results indicated that histone acetylation was required for the transcriptional activation of SSA3 and SSA4. The HATs (histone acetyltransferases) Gcn5 (general control non-derepressible 5) and Elp3 (elongation protein 3) modulated hsp70 gene transcription by affecting the acetylation status of histone H3. Although the two HATs possessed overlapping function regarding the acetylation of histone H3, they affected hsp70 gene transcription in different ways. The recruitment of Gcn5 was Swi/Snf-dependent and was required for HSF (heat-shock factor) binding and affected RNAPII (RNA polymerase II) recruitment, whereas Elp3 exerted its roles mainly through affecting RNAPII elongation. These results provide insights into the effects of Gcn5 and Elp3 in hsp70 gene transcription and underscore the importance of histone acetylation for transcriptional initiation and elongation in hsp genes.
Authors	Qiuju Han, Jun Lu, Jizhou Duan, Dongmei Su, Xiaozhe Hou, Fen Li, Xiuli Wang, Baiqu Huang
Journal	The Biochemical journal (Biochem J) Vol. 409 Issue 3 Pg. 779-88 (Feb 01 2008) ISSN: 1470-8728 [Electronic] England
PMID	17910533 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
Chemical References	HSP70 Heat-Shock Proteins Histones SSA3 protein, S cerevisiae SSA4 protein, S cerevisiae Saccharomyces cerevisiae Proteins Elp3 protein, S cerevisiae GCN5 protein, S cerevisiae Histone Acetyltransferases RNA Polymerase II
Topics	Acetylation HSP70 Heat-Shock Proteins (genetics, metabolism) Histone Acetyltransferases (genetics, metabolism) Histones (metabolism) RNA Polymerase II (metabolism) Saccharomyces cerevisiae (genetics, metabolism) Saccharomyces cerevisiae Proteins (genetics, metabolism) Transcription, Genetic (genetics)

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