Acetylation in histone H3 globular domain regulates gene expression in yeast
Acetylation in histone H3 globular domain regulates gene expression in yeast
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DOI：
10.1016/j.cell.2005.03.011
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发表时间：
2005-05-06
期刊：
影响因子：
64.5
通讯作者：
Grunstein, M
中科院分区：
文献类型：
--
作者：
Xu, F;Zhang, KL;Grunstein, M
在酿酒酵母中，已知的调节基因活性的组蛋白乙酰化位点位于从核小体核心突出的N-末端尾部。我们报告组蛋白H3中的赖氨酸56作为一种新的乙酰化位点，位于球状结构域中，当它缠绕在核小体周围时，它在DNA超螺旋的入口-出口点处向DNA大沟延伸。我们发现，K56乙酰化富集优先在某些活性基因，如编码组蛋白。SPT 10是一种公认的乙酰转移酶，是细胞周期特异性组蛋白基因K56乙酰化所必需的。这允许核小体重塑因子Snf 5的募集和随后的转录。这些发现表明，组蛋白H3 K56乙酰化的入口-出口门使招聘的SWI/SNF核小体重塑复合物，从而调节基因活性。
In Saccharomyces cerevisiae, known histone acetylation sites regulating gene activity are located in the N-terminal tails protruding from the nucleosome core. We report lysine 56 in histone H3 as a novel acetylation site that is located in the globular domain, where it extends toward the DNA major groove at the entry-exit points of the DNA superhelix as it wraps around the nucleosome. We show that K56 acetylation is enriched preferentially at certain active genes, such as those coding for histones. SPT10, a putative acetyltransferase, is required for cell cycle-specific K56 acetylation at histone genes. This allows recruitment of the nucleosome remodeling factor Snf5 and subsequent transcription. These findings indicate that histone H3 K56 acetylation at the entry-exit gate enables recruitment of the SWI/SNF nucleosome remodeling complex and so regulates gene activity.