Zhang Qing Yi, Zhang Ying Zi, Shen Kai, Zhang Shu Yu, Cao Jian Ping
School of Radiation Medicine and Protection, School for Radiological and Interdisciplinary Science, Soochow University, Suzhou 215123, China.
The First Clinical Medical School, Soochow University, Suzhou 215123, China.
Yi Chuan. 2019 Jan 20;41(1):29-40. doi: 10.16288/j.yczz.18-112.
Ubiquitylation is an essential type of protein post-translational modifications (PTMs) in eukaryotes, which mediates various biological processes by regulating the subcellular localization, activity, and stability of proteins. Histones, as the main protein ingredients of chromatin, are closely coupled with DNA activities such as replication, transcription and repair, and therefore are the hotspots of PTMs. After DNA damage, histone ubiquitylations are involved in DNA damage response (DDR) by regulating nucleosome structure, activating cell cycle checkpoints, remodeling the nucleosome, and the recruitment and assembly of repair factors. Meanwhile, histone ubiquitylations can also crosstalk with other types of PTMs to regulate DDR processes. In this review, we summarize how the site-specific histone ubiquitylation forms signal network and contributes to DDR, which may shed light on the further study of how histone codes formed by histone PTMs affect the entire DDR processes.
泛素化是真核生物中一种重要的蛋白质翻译后修饰（PTM）类型，它通过调节蛋白质的亚细胞定位、活性和稳定性来介导各种生物学过程。组蛋白作为染色质的主要蛋白质成分，与DNA的复制、转录和修复等活动密切相关，因此是PTM的热点。DNA损伤后，组蛋白泛素化通过调节核小体结构、激活细胞周期检查点、重塑核小体以及招募和组装修复因子参与DNA损伤反应（DDR）。同时，组蛋白泛素化还可以与其他类型的PTM相互作用，以调节DDR过程。在本综述中，我们总结了位点特异性组蛋白泛素化如何形成信号网络并促进DDR，这可能为进一步研究组蛋白PTM形成的组蛋白密码如何影响整个DDR过程提供线索。
