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Histone acetylation-independent transcription stimulation by a histone chaperone

机译:组蛋白伴侣不依赖组蛋白乙酰化的转录刺激

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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.
机译:组蛋白伴侣被认为对于维持组蛋白的生理活性很重要。但是,它们的确切作用尚不完全清楚。模板活化因子(TAF)-I(组蛋白伴侣之一)的生理功能也不清楚。但是,其生化特性已得到充分研究。通过进行微阵列分析,我们发现TAF-1刺激了基因亚集的转录。发现通过TAF-1上调的内源基因的转录被组蛋白乙酰化加性地刺激。在对包含整合到染色体中的模型基因的细胞系进行实验时,发现TAF-1以组蛋白伴侣活性依赖性方式刺激模型基因转录,并​​附加了组蛋白乙酰化作用。 TAF-1与核心组蛋白结合,并在体外重塑了染色质结构,独立于N端组蛋白尾巴及其乙酰化水平。这些结果表明TAF-1通过其与组蛋白的核心结构域(包括组蛋白折叠)的相互作用来重塑染色质结构,并且该机制与组蛋白乙酰化状态无关。

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