Plant vernalization proteins contain unusual PHD superdomains without histone H3 binding activity.

Plant vernalization proteins contain unusual PHD superdomains without histone H3 binding activity.
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DOI:
10.1016/j.jbc.2022.102540
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发表时间:
2022-11
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
Bienz M
Bienz M
中科院分区:
其他
文献类型:
--
作者:
Franco-Echevarría E;Rutherford TJ;Fiedler M;Dean C;Bienz M

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PHD指是染色质相关蛋白中的模块结构域,它解码组蛋白H3尾部的甲基化状态。在植物春化蛋白(VEL)中发现了PhD指状信号,这些蛋白作为Polycomb系统的辅助因子,通过表观遗传沉默机制控制拟南芥的开花。有人提出,VEL PHD手指与甲基化的组蛋白H3尾巴结合,以促进多梳沉默机制与靶基因的关联。在这里,我们使用X射线结晶学的结构分析来表明,VEL PhD指形成了一个更大的紧凑的三部分超域的中心模块,该超域还包含一个锌指和一个四螺旋束。这个PhD超域折叠只在另一个家族Oberon蛋白中发现,Oberon蛋白在拟南芥分生组织中具有控制植物生长的多种功能。Oberon蛋白假定的组蛋白结合表面显示出组蛋白结合PHD手指的特征三叉袋,并与甲基化的组蛋白H3尾巴结合。然而,Vel PhD Finger没有这种结构,并且表现出异常高的表面正电荷。等温量热法和核磁共振波谱表明,该Vel PhD超结构域既不与未修饰的组蛋白H3尾部结合,也不与不同程度修饰的组蛋白H3尾部结合。相反,VEL PhD超域与带负电荷的聚合物相互作用。我们的证据支持PHD超结构域在春化过程中的发散功能的进化,而不涉及组蛋白尾部的解码。
PHD fingers are modular domains in chromatin-associated proteins that decode the methylation status of histone H3 tails. A PHD finger signature is found in plant vernalization (VEL) proteins, which function as accessory factors of the Polycomb system to control flowering in Arabidopsis through an epigenetic silencing mechanism. It has been proposed that VEL PHD fingers bind to methylated histone H3 tails to facilitate association of the Polycomb silencing machinery with target genes. Here, we use structural analysis by X-ray crystallography to show that the VEL PHD finger forms the central module of a larger compact tripartite superdomain that also contains a zinc finger and a four-helix bundle. This PHD superdomain fold is only found in one other family, the OBERON proteins, which have multiple functions in Arabidopsis meristems to control plant growth. The putative histone-binding surface of OBERON proteins exhibits the characteristic three-pronged pocket of histone-binding PHD fingers and binds to methylated histone H3 tails. However, that of VEL PHD fingers lacks this architecture and exhibits unusually high positive surface charge. This VEL PHD superdomain neither binds to unmodified nor variously modified histone H3 tails, as demonstrated by isothermal calorimetry and NMR spectroscopy. Instead, the VEL PHD superdomain interacts with negatively charged polymers. Our evidence argues for evolution of a divergent function for the PHD superdomain in vernalization that does not involve histone tail decoding.
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