PHD 指结构域的非组蛋白结合功能。
Non-histone binding functions of PHD fingers.
机构信息
Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
出版信息
Trends Biochem Sci. 2023 Jul;48(7):610-617. doi: 10.1016/j.tibs.2023.03.005. Epub 2023 Apr 14.
Abstract
Plant homeodomain (PHD) fingers comprise a large and well-established family of epigenetic readers that recognize histone H3. A typical PHD finger binds to the unmodified or methylated amino-terminal tail of H3. This interaction is highly specific and can be regulated by post-translational modifications (PTMs) in H3 and other domains present in the protein. However, a set of PHD fingers has recently been shown to bind non-histone proteins, H3 mimetics, and DNA. In this review, we highlight the molecular mechanisms by which PHD fingers interact with ligands other than the amino terminus of H3 and discuss similarities and differences in engagement with histone and non-histone binding partners.
摘要
植物同源结构域 (PHD) 指包含一个庞大且成熟的组蛋白识别蛋白家族，可识别组蛋白 H3。典型的 PHD 指通过组蛋白 H3 的未修饰或甲基化氨基末端尾巴结合。这种相互作用具有高度特异性，并可通过 H3 及其在蛋白质中存在的其他结构域的翻译后修饰 (PTM) 进行调节。然而，一组 PHD 指最近已被证明可以与非组蛋白蛋白、H3 类似物和 DNA 结合。在这篇综述中，我们强调了 PHD 指与 H3 氨基末端以外的配体相互作用的分子机制，并讨论了与组蛋白和非组蛋白结合伙伴结合的异同。
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