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首页> 外文期刊>Molecular cell >The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition
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The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition

机译：yFACT Pob3-M结构域的结构，其与DNA复制因子RPA的相互作用以及在核小体沉积中的潜在作用

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摘要

We report the crystal structure of the middle domain of the Pob3 subunit (Pob3-M) of S. cerevisiae FACT (yFACT, facilitates chromatin transcription), which unexpectedly adopts an unusual double pleckstrin homology (PH) architecture. A mutation within a conserved surface cluster in this domain causes a defect in DNA replication that is suppressed by mutation of replication protein A (RPA). The nucleosome reorganizer yFACT therefore interacts in a physiologically important way with the central single-strand DNA (ssDNA) binding factor RPA to promote a step in DNA replication. Purified yFACT and RPA display a weak direct physical interaction, although the genetic suppression is not explained by simple changes in affinity between the purified proteins. Further genetic analysis suggests that coordinated function by yFACT and RPA is important during nucleosome deposition. These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process.
机译：我们报告了酿酒酵母FACT（yFACT，促进染色质转录）的Pob3亚基（Pob3-M）的中间结构域的晶体结构，它出人意料地采用了不同寻常的双pleckstrin同源性（PH）结构。该结构域中保守表面簇内的突变引起DNA复制缺陷，其被复制蛋白A（RPA）的突变抑制。因此，核小体重组子yFACT以生理上重要的方式与中央单链DNA（ssDNA）结合因子RPA相互作用，以促进DNA复制的一步。纯化的yFACT和RPA表现出较弱的直接物理相互作用，尽管遗传抑制不能通过纯化蛋白之间亲和力的简单变化来解释。进一步的遗传分析表明，yFACT和RPA的协调功能在核小体沉积过程中很重要。这些结果支持了FACT家族在DNA复制过程中构建核小体中起重要作用的模型，并表明RPA有助于这一过程。

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