YTHDF 蛋白冗余功能的结构与动态研究进展
Structural and Dynamic Insights into Redundant Function of YTHDF Proteins.
机构信息
Department of Biochemistry, University of Zurich, CH-8057 Zurich, Switzerland.
Department of Chemistry, Umeå University, SE-90187 Umeå, Sweden.
出版信息
J Chem Inf Model. 2020 Dec 28;60(12):5932-5935. doi: 10.1021/acs.jcim.0c01029. Epub 2020 Oct 19.
Three YTH-domain family proteins (YTHDF1, YTHDF2, and YTHDF3) recognize the N-methyladenosine (mA) modification of mRNA in cells. However, the redundancy of their cellular functions has been disputed. We investigate their interactions with mA-containing RNA using X-ray crystallography and molecular dynamics (MD). The new X-ray structures and MD simulations show that the three proteins share identical interactions with the mA-containing RNA and have similar intrinsic plasticity, thus evidencing the redundant roles of the three proteins in cellular functions.
三种 YTH 结构域家族蛋白（YTHDF1、YTHDF2 和 YTHDF3）在细胞中识别 mRNA 的 N6-甲基腺苷（m6A）修饰。然而，它们的细胞功能冗余性一直存在争议。我们使用 X 射线晶体学和分子动力学（MD）研究了它们与含 mA 的 RNA 的相互作用。新的 X 射线结构和 MD 模拟表明，这三种蛋白质与含 mA 的 RNA 具有相同的相互作用，并且具有相似的固有可塑性，从而证明了这三种蛋白质在细胞功能中具有冗余作用。
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