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Core Promoter Binding by Histone-Like TAF Complexes

机译:组蛋白样TAF复合物对核心启动子的结合

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A major function of TFIID is core promoter recognition. TFIID consists of TATA-binding protein (TBP) and 14 TBP-associated factors (TAFs). Most of them contain a histone fold domain (HFD) that lacks the DNA-contacting residues of histones. Whether and how TAF HFDs contribute to core promoter DNA binding are yet unresolved. Here we examined the DNA binding activity of TAF9, TAF6, TAF4b, and TAF12, which are related to histones H3, H4, H2A, and H2B, respectively. Each of these TAFs has intrinsic DNA binding activity adjacent to or within the HFD. The DNA binding domains were mapped to evolutionarily conserved and essential regions. Remarkably, HFD-mediated interaction enhanced the DNA binding activity of each of the TAF6-TAF9 and TAF4b-TAF12 pairs and of a histone-like octamer complex composed of the four TAFs. Furthermore, HFD-mediated interaction stimulated sequence-specific binding by TAF6 and TAF9. These results suggest that TAF HFDs merge with other conserved domains for efficient and specific core promoter binding.
机译:TFIID的主要功能是核心启动子识别。 TFIID由TATA结合蛋白(TBP)和14种TBP相关因子(TAF)组成。它们中的大多数含有缺乏组蛋白的DNA接触残基的组蛋白折叠结构域(HFD)。 TAF HFD是否以及如何促进核心启动子与DNA的结合尚无定论。在这里,我们检查了TAF9,TAF6,TAF4b和TAF12的DNA结合活性,它们分别与组蛋白H3,H4,H2A和H2B相关。这些TAF中的每一个都具有邻近HFD或在HFD内部的固有DNA结合活性。将DNA结合结构域定位到进化保守和必需区域。值得注意的是,HFD介导的相互作用增强了每个TAF6-TAF9和TAF4b-TAF12对以及由四个TAF组成的组蛋白样八聚体复合物的DNA结合活性。此外,HFD介导的相互作用刺激了TAF6和TAF9的序列特异性结合。这些结果表明TAF HFD与其他保守域合并有效和特异性的核心启动子绑定。

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