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首页> 外文期刊>Molecular and Cellular Biology >Two regions within the DNA binding domain of nuclear factor I interact with DNA and stimulate adenovirus DNA replication independently.
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Two regions within the DNA binding domain of nuclear factor I interact with DNA and stimulate adenovirus DNA replication independently.

机译：核因子I DNA结合域内的两个区域与DNA相互作用，并独立刺激腺病毒DNA复制。

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摘要

The cellular transcription factor nuclear factor I (NFI) stimulates adenovirus DNA replication by up to 50-fold. The NFI DNA binding domain (NFI-BD) is sufficient for stimulation and interacts with the viral DNA polymerase, thereby recruiting the precursor terminal protein-DNA polymerase complex (pTP-pol) to the origin of replication. The mechanism of DNA binding by NFI is unknown. To examine DNA binding and stimulation of adenovirus DNA replication by NFI-BD in more detail, we generated a series of deletion mutants and show that the DNA binding domain of NFI consists of two subdomains: a highly basic N-terminal domain that binds nonspecifically to DNA and a C-terminal domain that binds specifically but with very low affinity to the NFI recognition site. Both of these subdomains stimulate DNA replication, although not to the same extent as the intact DNA binding domain. The N-terminal domain has an alpha-helical structure, as shown by circular dichroism spectroscopy. The C-terminal domain interacts with the pTP-pol complex and is able to recruit the pTP-pol complex to DNA, which leads to pTP-pol-dependent stimulation of replication. The N-terminal domain also stimulates replication in a pTP-pol-dependent manner and enhances binding of pTP-pol to DNA. Since we could not detect a direct protein-protein interaction between pTP-pol and the N-terminal domain, we suggest that this domain stimulates replication by inducing structural changes in the DNA.
机译：细胞转录因子核因子I（NFI）最多可刺激腺病毒DNA复制50倍。 NFI DNA结合域（NFI-BD）足以刺激并与病毒DNA聚合酶相互作用，从而将前体末端蛋白质-DNA聚合酶复合物（pTP-pol）募集到复制起点。 NFI与DNA结合的机制尚不清楚。为了更详细地检查NFI-BD的DNA结合和腺病毒DNA复制的刺激，我们产生了一系列缺失突变体，并显示NFI的DNA结合结构域由两个亚结构域组成：一个高度碱性的N末端结构域，与非特异性结合DNA和与NFI识别位点特异性结合但亲和力极低的C端结构域。这两个亚域都刺激DNA复制，尽管程度不如完整的DNA结合域。 N末端结构域具有α-螺旋结构，如圆二色性光谱法所示。 C末端结构域与pTP-pol复合物相互作用并且能够将pTP-pol复合物募集至DNA，这导致pTP-pol依赖性复制的刺激。 N末端结构域还以pTP-pol依赖性方式刺激复制并增强pTP-pol与DNA的结合。由于我们无法检测到pTP-pol与N末端结构域之间的直接蛋白质相互作用，因此我们建议该结构域通过诱导DNA的结构变化来刺激复制。

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