Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland.
Trends Cell Biol. 2011 Sep;21(9):534-42. doi: 10.1016/j.tcb.2011.06.001. Epub 2011 Jul 7.
Most published work on post-translational histone modifications focuses on small covalent alterations such as acetylation, methylation and phosphorylation. By contrast, fewer data are available on the modification of histones by ADP-ribose. Discussion of the biological significance of histone ADP-ribosylation has often been restricted to functions of the modifying enzymes, rather than to histones as ADP-ribose acceptors. In particular, the identification of specific lysine residues as ADP-ribose acceptor sites in histones and the identification of ADP-ribose binding modules raise this modification to a par with acetylation, methylation or phosphorylation. We discuss here the functional aspects of histone ADP-ribosylation and its influence on DNA repair, replication and transcription.
大多数关于翻译后组蛋白修饰的已发表工作都集中在小的共价修饰上，如乙酰化、甲基化和磷酸化。相比之下，关于组蛋白通过 ADP-核糖修饰的信息较少。组蛋白 ADP-核糖基化的生物学意义的讨论通常仅限于修饰酶的功能，而不是组蛋白作为 ADP-核糖受体。特别是，确定组蛋白中特定赖氨酸残基作为 ADP-核糖受体位点以及确定 ADP-核糖结合模块将这种修饰与乙酰化、甲基化或磷酸化相提并论。在这里，我们讨论了组蛋白 ADP-核糖基化的功能方面及其对 DNA 修复、复制和转录的影响。
