Histone acetylation-independent transcription stimulation by a histone chaperone.
Histone acetylation-independent transcription stimulation by a histone chaperone.
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DOI：
10.1093/nar/gkl1077
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发表时间：
2007
影响因子：
14.9
通讯作者：
Nagata K
中科院分区：
文献类型：
--
作者：
Kato K;Miyaji-Yamaguchi M;Okuwaki M;Nagata K
组蛋白伴侣被认为对于维持组蛋白的生理活性很重要;然而，它们的确切作用尚不完全清楚。模板激活因子（TAF）-I的生理功能，组蛋白伴侣之一，也仍然不清楚，但是，它的生化特性已经得到了很好的研究。通过进行微阵列分析，我们发现TAF-I刺激一组基因的转录。被TAF-I上调的内源性基因的转录被发现被组蛋白乙酰化加成刺激。在用含有整合到染色体中的模型基因的细胞系进行实验时，发现TAF-I以组蛋白伴侣活性依赖性方式与组蛋白乙酰化相加地刺激模型基因转录。TAF-I与核心组蛋白结合，并在体外重塑染色质结构，而不依赖于N-末端组蛋白尾部及其乙酰化水平。这些结果表明，TAF-I通过与组蛋白的核心结构域（包括组蛋白折叠）相互作用来重塑染色质结构，并且这种机制与组蛋白乙酰化状态无关。
Histone chaperones are thought to be important for maintaining the physiological activity of histones; however, their exact roles are not fully understood. The physiological function of template activating factor (TAF)-I, one of the histone chaperones, also remains unclear; however, its biochemical properties have been well studied. By performing microarray analyses, we found that TAF-I stimulates the transcription of a sub-set of genes. The transcription of endogenous genes that was up-regulated by TAF-I was found to be additively stimulated by histone acetylation. On performing an experiment with a cell line containing a model gene integrated into the chromosome, TAF-I was found to stimulate the model gene transcription in a histone chaperone activity-dependent manner additively with histone acetylation. TAF-I bound to the core histones and remodeled the chromatin structure independent of the N-terminal histone tail and its acetylation level in vitro. These results suggest that TAF-I remodel the chromatin structure through its interaction with the core domain of the histones, including the histone fold, and this mechanism is independent of the histone acetylation status.
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