大分子拥挤增加了 ING4 的 PHD 结构域与组蛋白 H3K4me3 标记的亲和力。
Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark.
机构信息
CIC bioGUNE, Bizkaia Science and Technology Park, bld 800, 48160 Derio, Bizkaia, Spain.
IKERBASQUE, Basque Foundation for Science, Maria Diaz de Haro 3, 6 solairua, 48013 Bilbao, Bizkaia, Spain.
出版信息
Biomolecules. 2020 Feb 4;10(2):234. doi: 10.3390/biom10020234.
The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular crowding agent, the mode of binding does not change but the affinity increases by one order of magnitude. The affinity increases also for unmethylated histone H3 tail, but the difference with H3K4me3 is larger in the presence of Ficoll. These results indicate that in the cellular milieu, the affinity of the ING proteins for their chromatin target is larger than previously thought.
抑癌蛋白家族的五个成员包含一个植物同源结构域（PHD），该结构域特异性识别组蛋白 H3 赖氨酸 4 三甲基化（H3K4me3），亲和力在低微摩尔范围内。在这里，我们使用 NMR 表明，在惰性大分子拥挤剂 15%Ficoll 70 的存在下，结合模式没有改变，但亲和力增加了一个数量级。未甲基化的组蛋白 H3 尾部的亲和力也增加了，但在 Ficoll 存在下，与 H3K4me3 的差异更大。这些结果表明，在细胞环境中，ING 蛋白与其染色质靶标的亲和力大于先前的想象。
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