Han Qiuju, Lu Jun, Duan Jizhou, Su Dongmei, Hou Xiaozhe, Li Fen, Wang Xiuli, Huang Baiqu
Key Laboratory of Molecular Epigenetics of Ministry of Education, Institute of Genetics and Cytology, Northeast Normal University, Changchun 130024, China.
Biochem J. 2008 Feb 1;409(3):779-88. doi: 10.1042/BJ20070578.
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.
本研究的目的是阐明组蛋白乙酰化参与酵母中热休克蛋白70（hsp70）基因SSA3和SSA4转录调控的机制。我们的结果表明，组蛋白乙酰化是SSA3和SSA4转录激活所必需的。组蛋白乙酰转移酶（HATs）Gcn5（一般控制非抑制性5）和Elp3（延伸蛋白3）通过影响组蛋白H3的乙酰化状态来调节hsp70基因转录。尽管这两种HATs在组蛋白H3乙酰化方面具有重叠功能，但它们以不同方式影响hsp70基因转录。Gcn5的募集依赖于Swi/Snf，是热休克因子（HSF）结合所必需的，并影响RNA聚合酶II（RNAPII）的募集，而Elp3主要通过影响RNAPII延伸发挥作用。这些结果为Gcn5和Elp3在hsp70基因转录中的作用提供了见解，并强调了组蛋白乙酰化对hsp基因转录起始和延伸的重要性。
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