Histone ubiquitylation and its roles in DNA damage response
Received date: 2018-07-10
Revised date: 2018-09-04
Online published: 2018-10-19
Supported by
[Supported by the National Students’ Platform for Innovation and Entrepreneurship Training Program (Nos. 201610285039Z, 201610285045Z)]
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.
Key words： histone; ubiquitylation; DNA damage response (DDR); crosstalk
Qingyi Zhang, Yingzi Zhang, Kai Shen, Shuyu Zhang, Jianping Cao . Histone ubiquitylation and its roles in DNA damage response[J]. Hereditas(Beijing), 2019 , 41(1) : 29 -40 . DOI: 10.16288/j.yczz.18-112
| [1] | Mariñoramírez L, Kann MG, Shoemaker BA, Landsman D . Histone structure and nucleosome stability. Expert Rev Proteomic, 2005,2(5):719-729. [DOI] |
| [2] | Luger K, Mäder AW, Richmond RK, Sargent DF, Richmond TJ . Crystal structure of the nucleosome core particle at 2.8Å resolution. Nature, 1997,389(6648):251-260. [DOI] |
| [3] | Strahl BD, Allis CD . The language of covalent histone modifications. Nature, 2000,403(6765):41-45. [DOI] |
| [4] | Suganuma T, Workman JL . Crosstalk among histone modifications. Cell, 2008,135(4):604-607. [DOI] |
| [5] | Lee JS, Smith E, Shilatifard A . The language of histone crosstalk. Cell, 2010,142(5):682-685. [DOI] |
| [6] | Hershko A, Ciechanover A . The ubiquitin system. Annu Rev Biochem, 1998,67(1):425-479. [DOI] |
| [7] | Herrmann J, Lerman LO, Lerman A . Ubiquitin and ubiquitin-like proteins in protein regulation. Circ Res, 2007,100(9):1276-1291. [DOI] |
| [8] | Shaid S, Brandts CH, Serve H, Dikic I . Ubiquitination and selective autophagy. Cell Death Differ, 2013,20(1):21-30. [DOI] |
| [9] | Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C. A proteome-wide , quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles. Mol Cell Proteomics, 2011, 10(10): M111.013284. [DOI] |
| [10] | Welchman RL, Gordon C, Mayer RJ . Ubiquitin and ubiquitin-like proteins as multifunctional signals. Nat Rev Mol Cell Bio, 2005,6(8):599-609. [DOI] |
| [11] | Schnell JD, Hicke L . Non-traditional functions of ubiquitin and ubiquitin-binding proteins. J Biol Chem, 2003,278(38):35857-35860. [DOI] |
| [12] | Komander D, Rape M . The Ubiquitin Code. Annu Rev Biochem, 2012,81:203-229. [DOI] |
| [13] | Goldknopf IL, Taylor CW, Baum RM, Yeoman LC, Olson MO, Prestayko AW, Busch H . Isolation and characterization of protein A24, a "histone-like" non-histone chromosomal protein. J Biol Chem, 1975,250(18):7182-7187. [DOI] |
| [14] | Goldknopf IL, Busch H . Isopeptide linkage between nonhistone and histone 2A polypeptides of chromosomal conjugate-protein A24. Proc Natl Acad Sci USA, 1977,74(3):864-868. [DOI] |
| [15] | Wang H, Wang L, Erdjument-Bromage H, Vidal M, Tempst P, Jones RS, Zhang Y . Role of histone H2A ubiquitination in polycomb silencing. Nature, 2004,431(7010):873-878. [DOI] |
| [16] | Fang J, Chen TB, Li E, Zhang Y . Ring1b-mediated H2A ubiquitination associates with inactive X chromosomes and is involved in initiation of X inactivation. J Biol Chem, 2004,279(51):52812-52815. [DOI] |