Department of Pharmacology, University of Colorado School of Medicine, Aurora, Colorado, USA.
Nat Struct Mol Biol. 2012 Dec;19(12):1218-27. doi: 10.1038/nsmb.2436.
Post-translational modifications (PTMs) of histones provide a fine-tuned mechanism for regulating chromatin structure and dynamics. PTMs can alter direct interactions between histones and DNA and serve as docking sites for protein effectors, or readers, of these PTMs. Binding of the readers recruits or stabilizes various components of the nuclear signaling machinery at specific genomic sites, mediating fundamental DNA-templated processes, including gene transcription and DNA recombination, replication and repair. In this review, we highlight the latest advances in characterizing histone-binding mechanisms and identifying new epigenetic readers and summarize the functional significance of PTM recognition.
组蛋白的翻译后修饰(PTMs)为调节染色质结构和动力学提供了一种微调机制。PTMs 可以改变组蛋白与 DNA 之间的直接相互作用,并作为这些 PTM 的蛋白质效应物或“读取器”的对接位点。这些“读取器”的结合在特定基因组位点募集或稳定核信号转导机制的各种成分,介导包括基因转录和 DNA 重组、复制和修复在内的基本 DNA 模板过程。在这篇综述中,我们强调了在表征组蛋白结合机制和识别新的表观遗传读取器方面的最新进展,并总结了 PTM 识别的功能意义。