Fis蛋白从DNA上易化解离的分子机制
Molecular Mechanism of Facilitated Dissociation of Fis Protein from DNA.
作者信息
Tsai Min-Yeh, Zhang Bin, Zheng Weihua, Wolynes Peter G
机构信息
Department of Chemistry, and Center for Theoretical Biological Physics, Rice University , Houston, Texas 77005, United States.
Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.
出版信息
J Am Chem Soc. 2016 Oct 19;138(41):13497-13500. doi: 10.1021/jacs.6b08416. Epub 2016 Oct 5.
Fis protein is a nucleoid-associated protein that plays many roles in transcriptional regulation and DNA site-specific recombination. In contrast to the naïve expectation based on stoichiometry, recent single-molecule studies have shown that the dissociation of Fis protein from DNA is accelerated by increasing the concentration of the Fis protein. Because the detailed molecular mechanism of facilitated dissociation is still not clear, in this study, we employ computational methods to explore the binding landscapes of Fis:DNA complexes with various stoichiometries. When two Fis molecules are present, simulations uncover a ternary complex, where the originally bound Fis protein is partially dissociated from DNA. The simulations support a three-state sequential kinetic model (N ⇄ I → D) for facilitated dissociation, thus explaining the concentration-dependent dissociation.
Fis蛋白是一种类核相关蛋白，在转录调控和DNA位点特异性重组中发挥多种作用。与基于化学计量学的单纯预期相反，最近的单分子研究表明，增加Fis蛋白的浓度会加速Fis蛋白从DNA上的解离。由于促进解离的详细分子机制仍不清楚，在本研究中，我们采用计算方法来探索具有不同化学计量学的Fis:DNA复合物的结合态势。当存在两个Fis分子时，模拟发现了一种三元复合物，其中最初结合的Fis蛋白部分从DNA上解离。模拟结果支持促进解离的三态顺序动力学模型（N ⇄ I → D），从而解释了浓度依赖性解离。
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